Selection of scientific articles using the Bio-Logic rapid kinetics systems


Important note: please cite us as “Bio-Logic SAS” and possibly send us the information when your paper is published using our instrumentation.Updated : January 18, 2013 . Note: this list is not supposed to cover all articles published by our clients.

Stopped-flow (fluorescence, light scattering, absorbance)Rapid Collapse into a Molten Globule Is Followed by Simple Two-State Kinetics in the Folding of Lysozyme from Bacteriophage λ
Alexandre Di Paolo, Dorothee Balbeur, Edwin De Pauw, Christina Redfield, and Andre Matagne
Biochemistry 2010, 49, 8646–8657
(SFM400 + MOS450AF/CD)

Temperature and Solvent Effects on Radical Scavenging Ability of Phenols
Velmurugan Thavasi, Ryan Phillip Anthony Bettens, and Lai Peng Leong J. Phys. Chem. A, 2009, 113 (13), 3068-3077
(SFM-300 + MOS200 I)

Automated Cell-Based Assay for Screening of Aquaporin Inhibitors
Maria Grazia Mola, Grazia Paola Nicchia, Maria Svelto, David C. Spray and Antonio Frigeri
Anal. Chem., 2009, 81 (19), pp 8219–8229
(SFM-20 + J620 I Light scattering)

Binding kinetics of glucose and allosteric activators to human glucokinase reveal multiple conformational states
Antoine M, Boutin J A, Ferry G (2009)
Biochemistry, 2009, 48, 5466-5482
(SFM300 + MOS200M)

Identification of Alpha-1 Acid Glycoprotein as a Lysophospholipid Binding Protein: A Complementary Role to Albumin in the Scavenging of Lysophosphatidylcholine
Pauli J. Ojala, Martin Hermansson, Martti Tolvanen, Kirsi Polvinen, Tia Hirvonen, Ulla Impola, Matti Jauhiainen,Pentti Somerharju, and Jaakko Parkkinen
Biochemistry 2006, 45, 14021-14031
(SFM-20+ MOS-250)

Biochemical Characterization and Ligand Binding Properties of Neuroglobin, a Novel Member of the Globin Family
Sylvia Dewilde, Laurent Kiger, Thorsten Burmester,Thomas Hankeln, Veronique Baudin-Creuza, Tony Aerts, Michael C. Marden, Roland Caubergs, and Luc Moens
J. Biol. Chem., Vol. 276, Issue 42, 38949-38955, October 19, 2001
(SFM-3 + MOS-200)

Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation
Julie A. Hoy, Benoit J. Smagghe, Puspita Halder, and Mark S. Hargrove
Protein Science (2007), 16:250-260
(SFM-400+MOS-250 | Stopped-Flow & fluorescence)

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
Gerd P. Bienert, Kim A. Kristiansen, Ian M. Møller, and Thomas P. Jahn
J Biol. Chem. 2007 Jan 12;282(2):1183-92
(MOS-250+SFM-300 | Stopped-Flow & fluorescence+ light scattering)

Revisiting a proposed kinetic model for the reaction of cysteine and hydrogen peroxide via cysteine sulfenic acid
Michael T. Ashby , Péter Nagy
International Journal of Chemical Kinetics; Volume 39, Issue 1 , Pages 32 – 38
(SFM-400+MOS-450/AF | Stopped-flow + fluorescence/absorbance)

Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
Thomas R Jahn, Martin J Parker, Steve W Homans & Sheena E Radford
Nature, Structural and Molecular Biology, 13, 195 – 201 (2006)
(SFM-4 + MOS-450/AF-CD)

Polymerization of Anionic Wormlike Micelles
Zhiyuan Zhu, Yamaira I. Gonzalez, Hangxun Xu, Eric W. Kaler, and Shiyong Liu
Langmuir 2006, 22, 949-955
(SFM-300/S + MOS-250, light scattering)

A Stopped-Flow Kinetic Study of the Assembly of Interpolymer Complexes via Hydrogen-Bonding Interactions
Shizhong Luo, Shiyong Liu, Jian Xu, Hao Liu, Zhiyuan Zhu, Ming Jiang, and Chi Wu
Macromolecules, 2006; 39(13); 4517-4525
(SFM-300/S + MOS-250, light scattering)

First Observation of Two-Stage Collapsing Kinetics of a Single Synthetic Polymer Chain
Jian Xu, Zhiyuan Zhu, Shizhong Luo, Chi Wu, and Shiyong Liu
Physical Review Letters, 2006, 96, 027802
(SFM-300/S + MOS-250, light scattering, fluorescence)

Mechanism of a-oxoamine synthases: identification of the intermediate Claisen product in the 8-amino-7-oxononanoate synthase reaction
Olivier Kerbarh, Dominic J. Campopiano and Robert L. Baxter*
Chem. Commun., 2006, 60–62
(MOS-450/AF-CD + SFM-300)

Probing the Kinetics of Membrane-Mediated Helix Folding
Matthew J. Tucker, Jia Tang, and Feng Gai
J. Phys. Chem. B, 110 (15), 8105 -8109, 2006
(SFM-300+ microcuvette (fluorescence + FRET))

Tryptophan 243 affects interprotein contacts, cofactor binding and stability in D-amino acid oxidase from Rhodotorula gracilis
Laura Caldinelli, Gianluca Molla, Mirella S. Pilone and Loredano Pollegioni
FEBS journal – Volume 273 Page 504 – February 2006
(SFM-300 + Jasco FP-750)

Efficient Refolding of Aggregation-prone Citrate Synthase by Polyol Osmolytes HOW WELL ARE PROTEIN FOLDING AND STABILITY ASPECTS COUPLED?*
Rajesh Mishra, Robert Seckler, and Rajiv Bhat
THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 280, No. 16, Issue of April 22, pp. 15553-15560
(SFM-300 + J-810)

The mechanism of GroEL/GroES folding/refolding of protein substrates revisited
Huw Jones, Monika Preuss, Michael Wright and Andrew D. Miller
Organic & Biomolecular Chemistry, 2006, 4, 1223 – 1235
(SFM-3 + MOS-200)

Ribose 2′-hydroxyl groups in the 5′ strand of the acceptor arm of P-site tRNA are not essential for EF-G catalyzed translocation
JASON S. FEINBERG and SIMPSON JOSEPH
RNA (2006), 12:580-588
(SFM-20 + MOS-200)

Escherichia coli RecQ Is a Rapid, Efficient, and Monomeric Helicase
Xing-Dong Zhang, Ping Xie, Peng-Ye Wang, and Xu Guang Xi
J. Biol. Chem., Vol. 281, Issue 18, 12655-12663, May 5, 2006
(SFM-400 + MOS-450/AF-CD)

pH-Induced Micellization Kinetics of ABC Triblock Copolymers Measured by Stopped-Flow Light Scattering
Zhiyuan Zhu, Steven P. Armes, and Shiyong Liu
Macromolecules 2005, 38, 9803-9812
(SFM-300/S + MOS-250, light scattering)

Trifluoroethanol-Induced Unfolding of Concanavalin A: Equilibrium and Time-Resolved Optical Spectroscopic Studies
Qi Xu and Timothy A. Keiderling
Biochemistry, 44 (22), 7976 -7987, 2005
(SFM-400 + J-810)

Pore selectivity analysis of an aquaglyceroporin by stopped-flow spectrophotometry on bacterial cell suspensions.
Hubert JF, Duchesne L, Delamarche C, Vaysse A, Gueune H, Raguenes-Nicol
C. Biol Cell. 2005 Sep;97(9):675-86.
(SFM-300+MOS-250)

RecQ Helicase-catalyzed DNA unwinding detected by fluorescence resonance energy transfer
X-D.Zhang, S-X.Dou, P. Xie, P-Y Wang, X-G Xi
Acta biochimica et Piophysica Sinica 2005, 37(9): 593-600.
(MOS-450 AF/CD + SFM-400 fluorescence)

Computational redesign of protein-protein interaction specificity
T.Kortemme, L.Joachimiak, A.Bullock, A.Schuler, B.Stoddard, D.Baker
Nature Structural and Molecular Biology, Volume 11, Number 4, April 2004, 372-379
(SFM-4 + SPEX fluorolog)

The Heparin Binding Properties of Heparin Cofactor II Suggest an Antithrombin-like Activation Mechanism
Denis O’Keeffe, Nijole Gasiunas, John Gallagher, Trevor P. Baglin, and James A. Huntington J.
Biol. Chem., Vol. 279, Issue 48, 50267-50273, November 26, 2004
(MOS-450+SFM-300 : fluorescence)

Rapid mixing methods for exploring the kinetics of protein folding
H.Roder, K.maki, H.Cheng, M Ramachandra Shastry
Methods 34 (2004) 15-27.
(SFM-400+ microcuvette: dead time of 0.55 ms)

Stopped-flow and Mutational Analysis of Base Flipping by the Escherichia coli Dam DNA-(adenine- N6)-methyltransferase.
Kirsten Liebert, Andrea Hermann, Martina Schlickenrieder and Albert Jeltsch.
J. Mol. Biol. (2004) 341, 443-454
(SFM-3 + MOS-200)

Properties of some variants of human beta2-microglobulin and amyloidogenesis
A.Corazza,F.Pettirossi, P.Viglino, G.Verdone, J.Garcia, P.Dumy, S.Giorgetti, P.Mangione, S.raimondi, M.Stoppini, V.belloti, G.Esposito
Journal of Biological Chemistry, Vol.279, N°10, 9176-9189, 2004
(SFM-300 + fluorescence )

Probing the influence on folding behavior of structurally conserved core residues in P.Aerogonesa apo-azurin
K.C.Engman, A. Sandberg, J.Leckner, G. Karlsson
Protein Science (2004), 13, 2706-2715
(SFM-20 + MOS-450 in fluorescence mode)

Apo-azurin folds via an intermediate resembles the moten-globule
A.Sandberg, J.Leckner, BG. Karlsson
Protein Science (2004), 13, 2628-2638
(SFM-20 + MOS-250 + MOS-450 in fluorescence and CD mode)

DNA recognition by the Homing Endonuclease PI-SceI involves a divalent metal ion cofactor induced conformational change
AJ Noel, W. Wende, A.Pingoud
Journal of Biological Chemistry, Vol 279, N°8, 6794-6804, 2004
(SFM-300 + fluorescence)

Human Rhesus-associated glycoprotein mediates facilitated transport of NH3 into red blood cells
Pierre Ripoche, Olivier Bertrand, Pierre Gane, Connie Birkenmeier, Yves Colin, and Jean-Pierre Cartron
PNAS 2004 101: 17222-17227.
(SFM-3 + MOS-200 | light scattering + fluorescence + titrator)

Revisiting the role of H+ in chmotactic signaling of sperm
Solzin J., Helbig A., Van Q., Brown, J.E., Hildebrand E., Weyand I., Kaupp U.B.
The Journal of General Physiology, 2004, 124:115-124
(SFM-4/S + MOS-200 | Fluorescence)

The signal flow and motor response controling chemotaxis of sea urchin sperm.
Kaupp U.B., Solzin J., Hildebrand E., Brown, J.E., Helbig A., Hagen V., Beyermann M., Pampaloni F., Weyand I.
Nature Cell Biology 5 (2003) S. 109-117
(SFM-4/S + MOS-200 | Fluorescence)

Enzymatic mechanism of RNA translocation in dsRNA bacteriophages.
Lisal, J., Kainov, D. E., Bamford, D. H., Thomas, G. J., Jr., and Tuma R.
(2004). J. Biol. Chem., 279, 1343-1350
(SFM-20 + MOS-250 | Fluorescence )

Structural and kinetics characterization of the simplified SH3 domain FP1
Q.Yi, P.Rajagopal, R.Klevit, D.Baker
Protein Science (2003), 12: 776-783
(SFM-4 + MOS-200)

Amino Acids of the Bacterial Toxin SopE Involved in G Nucleotide Exchange on Cdc42
Markus C. Schlumberger <l >, Gretel Buchwald, Klaus Scheffzek , Alfred Wittinghofer , and Wolf-Dietrich Hardt
J. Biol. Chem., Vol. 278, Issue 29, 27149-27159, July 18, 2003
(SFM-20 + MOS-450 AF/CD | SF Fluorescence and steady state CD spectra)

The influence of hinge region residue Glu381 on antithrombin allostery and metastability.
Johnson DJ, Huntington JA.
J Biol Chem. 2003 Nov 17.
(SFM-300 & MOS-450 in fluorescence)

Catalytic Mechanism of the Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26.
Prokop, Z., Monincova, M., Chaloupkova, R., Klvana, M., Nagata, Y., Janssen, D.B., Damborsky, J.
2003: Journal of Biological Chemistry 278: 45094-45100.
(QFM-400 microvolume Quench-Flow & SFM-20+J-810 in Fluo)

Surface Expansion Is Independent of and Occurs Faster than Core Solvation during the Unfolding of Barstar
K. Sridevi and Jayant B. Udgaonkar*
Biochemistry 2003, 42, 1551-1563.
(SFM-400 & MOS-250 in fluorescence)

Characterization of Single-Tryptophan Mutants of Histidine-Containing Phosphocarrier Protein: Evidence for Local Rearrangements during Folding from High Concentrations of Denaturant
Azuaga, A. I.; Canet, D.; Smeenk, G.; Berends, R.; Titgemeijer, F.; Duurkens, R.; Mateo, P. L.; Scheek, R. M.; Robillard, G. T.; Dobson, C. M.; van Nuland, N. A. J.;
Biochemistry ; (Article); 2003; 42(17); 4883-4895.
(Stopped-Flow/CD with SFM-3 & MOS-400, Stopped-Flow/Fluorescence&Fluorescence Anisotropy with SFM-3 &  MOS-400 using the EMFA® method)

A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core.
F. Schäfer, D. Deluca, U. Majdic, J. Kirchner, M. Schliwa, L. Moroder and G. Woehlke
(SFM-3+ fluorescence)

Kinetic and Structural Characterization of Adsorption-induced Unfolding of Bovine Þ-Lactalbumin
Maarten F. M. Engel, Carlo P. M. van Mierlo, and Antonie J. W. G. Visser
J. Biol. Chem., Mar 2002; 277: 10922 – 10930.
(SFM-400)

Kinetic Analysis of R67 Dihydrofolate Reductase Folding: From the Unfolded Monomer to the Native Tetramer
Christophe Bodenreider, Nicolas Kellershohn, Michel E. Goldberg, and Annick Méjean
Biochemistry ; 2002; 41(50); 14988-14999.
(SFM-300 + MOS components + Jobin-Yvon CD6)

Role of individual disulfide bonds in hen lysozyme early folding steps
Valérie Guez, Pascale Roux, Amiel Navon and Michel E. Goldberg Protein Science (2002), 11:1136-1151.
(SFM-300 + MOS components + Jobin-Yvon CD6)

Immunochemical pulsed-labeling characterization of intermediates during hen lysozyme oxidative folding
Nicole M. Jarrett1, Lisa Djavadi-Ohaniance, Richard C. Willson, Hideki Tachibana and Michel E. Goldberg
Protein Science (2002), 11:2584-2595.
(SFM-300 + MOS components + Jobin-Yvon CD6)

The water permeability of Arabidoposis plasma membrane is regulated by divalent cations and pH
P. Gerbeau, G. Amodeo, T. Henzler, V. Santoni, P. Ripoche, C. Maurel
The plant Journal (2002) 30(1), 71-81.
(SFM-3+ light scattering)

Comparative trajectories of active and S195A inactive trypsin upon binding to serpins.
Mellet P, Mely Y, Hedstrom L, Cahoon M, Belorgey D, Srividya N, Rubin H, Bieth JG.
J Biol Chem. 2002 Oct 11;277(41):38901-14.
(SFM-3 + fluorescence (FRET))

Probing the DNA Interface of the EcoRV DNA-(Adenine-N6)-methyltransferase by Site-Directed Mutagenesis, Fluorescence Spectroscopy, and UV
Carsten Beck and Albert Jeltsch
Cross-Linking Biochemistry, (2002) 41 (48), 14103 -14110.
(SFM-3)

Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
Teilum K, Maki K, Kragelund BB, Poulsen FM, Roder H.
Proc Natl Acad Sci U S A. 99(15):9807-12. (2002).
(SFM-4)

The Two ADF-H Domains of Twinfilin Play Functionally Distinct Roles in Interactions with Actin Monomers
Pauli J. Ojala, Ville O. Paavilainen, Maria K. Vartiainen, Roman Tuma, Alan G. Weeds and Pekka Lappalainen
Molecular Biology of the Cell, Vol. 13, 3811-3821, November 2002
(MOS-250 + SFM-20)

Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects
Bryan A. Krantz1, Alok K. Srivastava, Sehat Nauli, David Baker, Robert T. Sauer & Tobin R. Sosnick
Nature Structural Biology June 2002 Volume 9, pp 458 – 463
(SFM-4/S et Q)

Kinetic Characterization of the pH-Dependent Oligomerization of R67 Dihydrofolate Reductase
Mejean, A.; Bodenreider, C.; Schuerer, K.; Goldberg, M. E.
Biochemistry ; 2001; 40(27); 8169-8179.
(SFM-300 + MOS components + Jobin-Yvon CD6)

Circularization Changes the Folding Transition State of the src SH3 Domain
Viara P. Grantcharova, David Baker
J.Mol.Biol. 2001, 306, 555-563
(SFM-400/MOS-400 Fluo)

Detection of Two Partially Structured Species in the Folding Process of the Amyloidogenic Protein 2-Microglobulin
Fabrizio Chiti, Palma Mangione, Alessia Andreola, Sofia Giorgetti, Massimo Stefani, Christopher M. Dobson, Vittorio Bellotti, Niccolò Taddei
J.Mol.Biol. 2001, 307, 379-391
(SFM-300/ MOS-400 Fluo / CD / double Jump)

Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype B.
Do-Hyung Kim, Gyu Hyun Nam, Do Soo Jang, Sunggoo Yun, Gildon Choi, Hee Cheon Lee and Kwan Yong Choi
Protein Science (2001), 10:741-752.
(SFM-400 + MOS-400/CD)

High dilutions with SFM-400 Concentration Jump Experiments for the Precise Determination of Rate Constants of Reverse Reactions in the Millisecond Time Range
P. Buet, E. Lewitzki, E. Grell, A.-M. Albrecht-Gary, K. J. Wannowius, F. Mass, H. Elias, A. A. Mundt & Y. Dupont
Analytical Chemistry 2001, 73, 857-863.
(SFM-400)

Structural and kinetic characterization of early folding events in-lactoglobulin
Kazuo Kuwata, Ramachandra Shastry, Hong Cheng, Masaru Hoshino, Carl A. Batt, Yuji Goto & Heinrich Roder
Nature Structural Biology February 2001 Volume 8 Number 2 pp 151 – 155
(SFM-400 + fluorescence)

The Dual-Specific Cdc25B Phosphatase: In Search of the Catalytic Acid.
Chen, W., Wilborn, M., Rudolph, J.
(2000) Biochemistry 39, 10781-10789
(SFM-400 + fluorescence)

Molecular Enzymology of the EcoRV DNA-(Adenine-N 6)-Methyltransferase: Kinetics of DNA Binding and Bending, Kinetic Mechanism and Linear Diffusion of the Enzyme on DNA
H. Gowhera and A. Jeltsch
Journal of Molecular Biology (2000) 303(1) 93-110

Enzymology with SFM-3 variable ratio Kinetic cooperativity of human liver alcohol dehydrogenase gamma-2.
Charlier HA, Plapp BV
J Biol Chem 2000 275:16 11569-75.
(SFM-3)

Equilibrium and Kinetic Analysis of Folding of Ketosteroid Isomerase from Comamonas testosteroni
Do-Hyung Kim, Do Soo Jang, Gyu Hyun Nam, Sunggoo Yun, Jae Hyun Cho, Gildon Choi, Hee Cheon Lee, and Kwan Yong Choi*
Biochemistry; 2000; 39(42); 13084-13092.
(SFM-4/QS, CD + fluorescence)

Long-range order in the src SH3 folding transition state
Viara P. Grantcharova, David S. Riddle, and David Baker
PNAS, Vol. 97, Issue 13, 7084-7089, June 20, 2000.
(SFM-4 + fluorescence)

Absence of stable intermediates on the folding pathway of barnase Takei, L.,Chu, RA, Bai, YW
PNAS 97 (20) 10796-10801 (2000).
(SFM-400 + MOS-400, CD + fluorescence)

Distinguishing between Two-State and Three-State Models for Ubiquitin Folding Bryan A. Krantz and Tobin R. Sosnick
Biochemistry 2000, 39, 11696-11701
(SFM-400, fluorescence single and double jump refolding)

Folding Kinetics of Phage 434 Cro Protein
D. V. Laurents, S. Corrales,  M. Eli´as-Arnanz, P. Sevilla, M. Rico, and S. Padmanabhan
Biochemistry 2000, 39, 13963-13973.
(SFM-4 + Fluorescence)

Evidence That Translocation of the Proteinase Precedes Its Acylation in the Serpin Inhibition Pathway
P. Mellet and JG Bieth
J. Biol. Chem. (2000) 275, pp. 10788-10795.
(SFM-3 + Fluorescence (FRET))

Cytochrome c folds through a smooth funnel
MARKANDESWAR PANDA, MARIA G. BENAVIDES-GARCIA, MICHAEL M. PIERCE, 1 and BARRY T. NALL
Protein Science (2000), 9: 536-543
(SFM-3 + optics)

D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding
Bryan A. Krantz, Liam B. Moran, Alex Kentsis & Tobin R.Sosnick
Nature Structural Biology Vol. 7, 62 – 71(2000)
(SFM-4 + PTI optics)

Kinetic evidence for the formation of a Michaelis-Menten-like complex between horseradish peroxidase compound II and di-(N-acetyl–tyrosine)
Weichi WANG, Stéphanie NOËL, Michel DESMADRIL, Jacques GUÉGUEN and Thierry MICHON
Biochem. J. (1999) 340, 329-336.
(SFM-3 + optics)

Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil.
Bhattacharyya, R.P. & Sosnick, T.R.
Biochemistry 8, 2601-2609 (1999)
(SFM-4 + PTI optics)

Control of Coenzyme Binding to Horse Liver Alcohol Dehydrogenase
Laurie A. LeBrun and Bryce V. Plapp
Biochemistry, 38 (38), 12387 -12393, 1999.
(SFM-3 + MOS-1000)

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
Jose C. Martínez & Luis Serrano
Nature Structural Biology, 1999 Volume 6 pp 1010 – 1016
(SFM-3)

Experiment and theory highlight role of native state topology in SH3 folding
David S. Riddle, Viara P. Grantcharova1, Jed V. Santiago, Eric Alm, Ingo Ruczinski & David Baker
Nature Structural Biology 1999 Volume 6 11 pp 1016 – 1024
(SFM-4)

Identifying the Site of Initial Tertiary Structure Disruption during Apomyoglobin Unfolding
Zhaoyang Feng, Jeung-Hoi Ha, and Stewart N. Loh
Biochemistry, 38 , 14433 -14439, 1999.
(SFM-4/QS).

Relationship between the Native-State Hydrogen Exchange and the Folding Pathways of Barnase
Rui-Ai Chu, Jiro Takei, Joseph J. Barchi, Jr., and Yawen Bai
Biochemistry, 38 (43), 14119 -14124, 1999.
(SFM-4/QS).

Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
Soon-Ho Park, M.C. Ramachandra Shastry & Heinrich Roder
Nature Structural Biology (1999) Vol. 6 pp 943 – 947
(SFM-4/QS).

Molecular Dissection of the Folding Mechanism of the R Subunit of Tryptophan Synthase: An Amino-Terminal Autonomous Folding Unit Controls Several Rate-Limiting Steps in the Folding of a Single Domain Protein
Jill A. Zitzewitz and C. Robert Matthews
Biochemistry 1999, 38, 10205-10214
(Fluorescence & CD with SFM-3 + Aviv CD + MOS-200).

Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants
Denis Canet, Margaret Sunde, Alexander M. Last, Andrew Miranker, Andrew Spencer, Carol V. Robinson, and Christopher M. Dobson
Biochemistry, 38 (20), 6419 -6427, 1999
(Fluorescence & CD with SFM-4).

Stopped-Flow Kinetic Analysis of the Ligand-Induced Coil-Helix Transition in Glutathione S-Transferase A1-1: Evidence for a Persistent Denatured State
Brenda S. Nieslanik, Michael J. Dabrowski, Robert P. Lyon, and William M. Atkins
Biochemistry, 38 (21), 6971 -6980, 1999
(Fluorescence with SFM-4).

Time-Resolved Monitoring of Electrogenic Na+ – Ca2+ Exchange in the Isolated Cardiac Sarcolemma Vesicles by Using a Rapid-Response Fluorescent Probe.
David Baazov, Xiolan Wang, and Daniel Khananshvili
Biochemistry (1999), 38, 1435-1445
(Fluorescence with SFM-3 + MOS-200)

Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c
YAWEN BAI
PNAS Vol. 96, pp. 477-480, 1999
(Fluorescence with SFM-4)

A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes.
Lagrée V, Pellerin I, Hubert JF, Tacnet F, Le Cahérec F, Roudier N, Thomas D, Gouranton J, Deschamps S
J Biol Chem 1998 May 15 273:20 12422-6
(SFM-3 + light scattering)

Evidence for the presence of aquaporin-3 in human red blood cells.
Roudier N, Verbavatz JM, Maurel C, Ripoche P, Tacnet F
J Biol Chem 1998 Apr 3 273:14 8407-12
(SFM-3 + light scattering)

Identification of a structural determinant for resistance to beta-lactam antibiotics in Gram-positive bacteria
N. MOUZ ,E. GORDON , A.-M. DI GUILMI ,I. PETIT ,Y. PETILLOT ,Y. DUPONT ,R. HAKENBECK ,T. VERNET , AND O. DIDEBERG
PNAS Vol. 95, pp. 13403-13406, 1998
(Fluorescence with SFM-3)

Limited internal friction in the rate-limiting step of a two-state protein folding reaction
Kevin W. Plaxco and David Baker.
PNAS Vol. 95, 13591-13596, 1998
(Fluorescence with SFM-4)

Initial hydrophobic collapse is not necessary for folding RNase A
Angela Nöppert, Klaus Gast, Dietrich Zirwer and Gregor Damaschun.
Folding & Design 1998, 3:213-221
(CD with SFM-3 + Jasco J-720 and Light scattering)

Probing the folding pathway of a -clam protein with single-tryptophan constructs
Patricia L Clark, Benjamin F Weston, Lila M Gierasch.
Folding & Design 1998, 3:401-412
(Fluorescence with SFM-4 + PTI and CD with SFM-4 + Jasco J-715).

Intrinsic tryptophans of CRABPI as probes of structure and folding
PATRICIA L. CLARK, ZHI-PING LIU, JIANHUA ZHANG, and LILA M. GIERASCH.
Protein Science (1996), 5: 1108- 1117
(Fluorescence with SFM-4 + PTI).

Mechanism of Folding of the Dimeric Core Domain of Escherichia coli Trp Repressor: A Nearly Diffusion-Limited Reaction Leads to the Formation of an On-Pathway Dimeric Intermediate
Lisa M. Gloss and C. Robert Matthews.
Biochemistry 1998, 37, 15990-15999
(Fluorescence + CD with SFM + MOS + Aviv CD)

SecB Binds Only to a Late Native-like Intermediate in the Folding Pathway of Barstar and Not to the Unfolded State
Vikram G. Panse, Jayant B. Udgaonkar, and Raghavan Varadarajan.
Biochemistry 1998, 37, 14477-14483
(Fluorescence with SFM-3 + MOS-200)

Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding
Alex Kentsis and Tobin R. Sosnick.
Biochemistry 1998, 37, 14613-14622
(Fluorescence + CD with SFM-3 + SFM-4 + MOS-200 + Jasco)

Evidence for an unfolding and refolding pathway in cytochrome c
Yujia Xu, Leland Mayne & S. Walter Englander.
Nature Structural Biology, 1998, Volume 5, pp 774 – 778

Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
Viara P. Grantcharova, David S. Riddle, Jed V. Santiago & David Baker.
Nature Structural Biology, 1998, Volume 5, pp 714 – 720

Obligatory steps in protein folding and the conformational diversity of the transition state
Jose C. Martinez, M. Teresa Pisabarro & Luis Serrano.
Nature Structural Biology, 1998, Volume 5, pp 721 – 729

Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange
Jeung-Hoi Ha & Stewart N. Loh.
Nature Structural Biology, 1998, Volume 5, pp 730 – 737

Evidence for barrier-limited protein folding kinetics on the microsecond time scale
M.C.Ramachandra Shastry and Heinrich Roder.
Nature Structural Biology, 1998 Volume 5 p385-391

Proline Isomerization-Independent Accumulation of an Early Intermediate and Heterogeneity of the Folding Pathways of a Mixed R/â Protein, Escherichia coli Thioredoxin
Roxana E. Georgescu, Jian-Hua Li, Michel E. Goldberg, Maria Luisa Tasayco, and Alain F. Chaffotte.
Biochemistry 1998, 37, 10286-10297

Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force
WILLIAM A. McGEE and BARRY T. NALL.
Protein Science (1998), 7: 1071-1082

Multiple Kinetic Intermediates Accumulate during the Unfolding of Horse Cytochrome c in the Oxidized State
Abani K. Bhuyan and Jayant B. Udgaonkar.
Biochemistry (1998), 37, 9147-9155

Stopped Flow Fluorescence Energy Transfer Measurement of the Rate Constants Describing the Reversible Formation and the Irreversible Rearrangement of the Elastase-alpha 1-Proteinase Inhibitor Complex
Philippe Mellet, Christian Boudier, Yves Mely, Joseph G.Bieth.
J. Biol. Chem. 1998 273 (15): p. 9119-9123

Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles
Teresa J. T. Pinheiro,* Gülnur A. Elöve, Anthony Watts, and Heinrich Roder.
Biochemistry, 36 (42), 13122 -13132, 1997.

An Early Intermediate in the Folding Reaction of the B1 Domain of Protein G Contains a Native-like Core
Soon-Ho Park, Karyn T. O’Neil, and Heinrich Roder.
Biochemistry, 36 (47), 14277 -14283, 1997.

Multiple intermediates and transition states during protein unfolding
Faisal N. Zaidi, Utpal Nath and Jayant B. Udgaonkar.
Nature Structure Biology Volume 4 Number 12 – December 1997

Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: A dynamic light scattering study
K Gast, D Zirwer, H Damaschun, U Hahn, M MullerFrohne, M Wirth, G Damaschun
FEBS Letters, 1997, Vol 403, Iss 3, pp 245-248

Stopped flow dynamic light scattering as a method to monitor compaction during protein folding
K Gast, A Noppert, M MullerFrohne, D Zirwer, G Damaschun
European Biophysics Journal with Biophysics Letters, 1997, Vol 25, Iss 3, pp 211-219

Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities
E LopezHernandez, P Cronet, L Serrano, V Munoz
Journal of Molecular Biology, 1997, Vol 266, Iss 3, pp 610-620

Favourable native-like helical local interactions can accelerate protein folding
AR Viguera, V Villegas, FX Aviles, L Serrano
Folding & Design, 1997, Vol 2, Iss 1, pp 23-33

Kinetic mechanism of luciferase subunit folding and assembly
AC Clark, SW Raso, JF Sinclair, MM Ziegler, AF Chaffotte, TO Baldwin
Biochemistry, 1997, Vol 36, Iss 7, pp 1891-1899

Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L
ML Scalley, Q Yi, HD Gu, A McCormack, JR Yates, D Baker
Biochemistry, 1997, Vol 36, Iss 11, pp 3373-3382

Fast folding of cytochrome c
MM Pierce, BT Nall
Protein Science, 1997, Vol 6, Iss 3, pp 618-627

The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
TM Raschke, S Marqusee
Nature Structural Biology, 1997, Vol 4, Iss 4, pp 298-304

Kinetic evidence for folding and unfolding intermediates in Staphylococcal nuclease
W.F. Walkenhorst, S.M. Green, H. Roder
1997, Biochemistry, 36:5795-5805

O-TRENSOX, a New Tripodal Iron Chelator Based on 8-Hydroxyquinoline Subunits: Thermodynamic and Kinetic Studies
Guy Serratrice, Hakim Boukhalfa, Claude Béguin, Paul Baret, Catherine Caris, and Jean-Louis Pierre
Inorganic Chemistry, 36, 3898-3910 (1997)

Kinetic Mechanism of Folding and Unfolding of Rhodobacter capsulatus Cytochrome c2
J. Michael Sauder, Neil E. MacKenzie, and Heinrich Roder
Biochemistry, 35 (51), 16852 -16862, 1996.

Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome-c folding
Colon, W., Elove, G.A., Wakem, L.P., Sherman, F. and Roder, H.
(1996) Biochemistry, 35, 5538-5549.

Kinetic intermediates in the formation of the cytochrome C
Colon, W. and Roder, H.
(1996) Nature Structural Biology 3, 1019-1025

Rapid interaction of FRCRCFa with the cytosolic side of the cardiac sarcolemma Na-Ca exchanger blocks the ion transport without preventing the binding of either sodium or calcium
Khananshvili, D., Baazov, D., Weil-Maslansky, E., Shaulov, G. and Mester, B.
(1996) Biochemistry, 35, 15933-15940

Conformational changes in the junctional foot protein/Ca2+ release channel mediate depolarization-induced Ca2+ release from sarcoplasmic reticulum
Yano, M., El-Hayek, R. k Ikemoto, N.
(1995) J. Biol. Chem. 270, 3017-3021

A kinetic scheme for the early phase of ATP hydrolysis by actomyosin ATPase and its bioenergetic implications.
Khan, L., A. And Amin, M.
(1995), Indian J. Biochem. Biophys. 32, 37-43

The folding mechanism of Barstar: evidence for multiple pathways and multiple intermediates
Shastry, M.C.R., and Udgaonkar, J.B.
(1995) J. Mol. Biol. 247, 1013-1027

A conformational change in the junctional foot protein is involved in the regulation of Ca’ release from sarcoplasmic reticulum. Studies on polylysine-induced Ccr” release.
El-Hayek, R., Yano, M. k Ikemoto, N.
(1995) J. Biol. Chem. 270, 15634-15638.

Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor.
El-Hayek, R., Antoniu, B., Wang, J., Hamilton, S.L. k Ikemoto, N.
(1995) J. Biol. Chem. 270, 22116-22118.

Binding of Ca²+ to the (Ca²+-Mg²+)-ATPase of sarcoplasmic reticulum: kinetic studies
Henderson, I.M.J., Starling, A.P., Wictome, M., East, J.M. and Lee, A.G.
(1994) Biochem. J. 297, 625-636.

Rapid refolding of native epitopes on the surface of cytochrome c.
Allen, M.J., Jemmerson, R. and Nail, B.T.
(1994), Biochemistry, 33, 3967-3973.

The barriers in protein folding
Sosnick, T.R., Mayne, L., Hiller, R. and Englander, S.W.
(1994) Nature Structural Biology 1, 149-155.

Tertiary interactions in the folding pathway of Hen lysozyme: kinetic studies using fluorescent probes
Itzhaki, L.S., Evans, P.A., Dobson, C.M. and Radford, S. E.
(1994) Biochemistry, 33, 5212-5220

Kinetic consequences of the removal of a disulfide bridge on the folding of Hen lysozyme
Eyles, S.J., Radford, S.E., Robinson, C.V. and Dobson, C.M.
(1994) Biochemistry, 33, 13038-13048

Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetics experiments.
Otto, M.R., Lillo, M.P. and Beechem, J.M.
(1994) Biophysical J. 67, 2511-2521

Kinetic characterization of the chemotactic protein from E. Coli, Che Y. Kinetic analysis of the inverse hydrophobic effect.
Munoz, V., Lopez, E.M., Jager, M. and Serrano, L.
(1994) Biochemistry, 33, 5858-5866

Chemical depolarization-induced SR calcium release in triads isolated from rabbit skeletal muscle
Ikemoto, N., Yano, M., El-Hayek, R., Antoniu, B. & Morii, M.
(1994) Biochemistry, 33, 10961-10968

Substrate Specificity of Alcohol Dehydrogenases.
Plapp, B.V., Green, D.W., Sun, H.W., Park, I.H., and Kim, K.
(1993) Enzymology and Molecular Biology of Carbonyl Metabolism 4, 391-400.

A Re-Examination of Folding Mechanism of DHFR from E-Coli Verification and Refinement of a Four Channel Model.
Jennings, P., Finn, B., Jones, B., Matthews, C.R.
(1993) Biochemistry, V.32, 3783-3789.

Alternative pathways and reactions of benzyl alcohol and benzaldehyde with horse liver alcohol dehydrogenase
Shearer, G.L., Kim, K., Lee, K. M., Wang, C.W. and Plapp, B.V.
(1993) 32, 11186-11194

Ca²+ binding to sarcoplasmic reticulum ATPase revisited. Equilibrium and kinetic evidence for a two route mechanism.
Forge, V., Mintz, E. and Guillain, F.
(1993) J. Biol. Chem. 268, 10961-10968.

Proton liberation in the pre-steady state phase of creatine kinase
Pal, P., K., Khan, L., A. and Amin, M.
(1993) Indian J. Biochem. Biophys. 30, 214-217

A reexamination of the stopped-flow measured hydrogen-deuterium exchange rates in nucleic acid double helices
Girardet, J.L. k Ramstein
(1992) Bioch. Bioph. Acta, 1130, 127-132.

A rapid-kinetic study of the class c B-lactamase of Enterobacter cloacae 908R.
Monnaie, D., Virden, R,, and Frere, J.M.
(1992), FEBS, Vol. 306, number 2.3, 108-112.

Determination of rate constants for nucleotide dissociation from Na, K ATPase.
Esmann, M.
(1992) Biochimica et Biophysica Acta, Vol. 1110, 20-28;

Effects of phospholipids on the function of (Ca2+-Mg2+)-ATPase
Michelangeli, F., Grimes, E.A., East, J.M. and Lee, A.G.
(1991) Biochemistry, 30, 342-351.

Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase.
Moutin, M.J. et Dupont, Y.
(1991), J. Biol. Chem. 266, 5580-5586

Determination of solute reflection coefficients in kidney brush-border membranes vesicles by light scattering: influence of refractive index.
Van der Goot, F., Ripoche, P. and Corman, B.
(1989), BBA Report, 979, 272-274.

Evidence of a calcium-induced structural change in the ATP-binding site of the sarcoplasmic reticulum Ca-ATPase using terbium formycin triphosphate as an analogue of Mg-ATP
Girardet, J.L., Dupont, Y. and Lacapere, J.J.
(1989) Eur. J. Biochem. 184, 131-140.

TOP 

Stopped-flow (circular dichroism)

Rapid Collapse into a Molten Globule Is Followed by Simple Two-State Kinetics in the Folding of Lysozyme from Bacteriophage λ
Alexandre Di Paolo, Dorothee Balbeur, Edwin De Pauw, Christina Redfield, and Andre Matagne
Biochemistry 2010, 49, 8646–8657
(SFM400 + MOS450AF/CD)

pH (low) insertion peptide (pHLIP) inserts across a lipid bilayer as a helix and exits by a different path
Oleg A. Andreev, Alexander G. Karabadzhak, Dhammika Weerakkody Gregory O. Andreev, Donald M. Engelman , and Yana K. Reshetnyak
PNAS March 2, 2010 vol. 107 no. 9 4081-4086
(SFM-300 + MOS-450AF/CD)

Structural Characterization of Apomyoglobin Self-Associated Species in Aqueous Buffer and Urea Solution
Charles Chow , Nese Kurt *, Regina M. Murphy and Silvia Cavagnero
Biophysical Journal 90:298-309 (2006)
(MOS-450/AF-CD + SFM-400 | CD stopped-flow and CD steady state mode)

Trifluoroethanol-Induced Unfolding of Concanavalin A: Equilibrium and Time-Resolved Optical Spectroscopic Studies
Qi Xu and Timothy A. Keiderling
Biochemistry, 44 (22), 7976 -7987, 2005
(SFM-400 + J-810)

Stabilization of Native Protein fold by intein-mediated covalent cyclization
N.Williams, E.liepinsh, S.Watt, P.Prosselkov, J.Matthews, P.Attard, J.Beck, N.Dixon, G.Otting
L.Mol.Biol.(2005) 346, 1095-1108
(SFM-300 + J-810)

Cooperative Sub-Millisecond Folding Kinetics of Apomyoglobin pH 4 Intermediate
Sebastien Weisbuch, Francine Gérard, Marielle Pasdeloup, Jéremy Cappadoro, Yves Dupont, and Marc Jamin
Biochemistry 2005, 44, 7013-7023.
(MOS-450AF/CD + SFM-400+microcuvette)

Apo-azurin folds via an intermediate resembles the moten-globule
A.Sandberg, J.Leckner, BG. Karlsson
Protein Science (2004), 13, 2628-2638
(SFM-20 + MOS-250 + MOS-450 in fluorescence and CD mode)

Secondary structure formation is the earliest structural event in the refolding of an all beta-sheet protein
T.Sivaraman, T.Kumar, Y.Tu, W.Wang, W.Lin, H.Chen, C.Yu
Biochemical and Biophysical research communications, 260, 284-288 (1999).
(SFM-3+J-720)

Characterization of Single-Tryptophan Mutants of Histidine-Containing Phosphocarrier Protein: Evidence for Local Rearrangements during Folding from High Concentrations of Denaturant
Azuaga, A. I.; Canet, D.; Smeenk, G.; Berends, R.; Titgemeijer, F.; Duurkens, R.; Mateo, P. L.; Scheek, R. M.; Robillard, G. T.; Dobson, C. M.; van Nuland, N. A. J.;
Biochemistry ; (Article); 2003; 42(17); 4883-4895.
(Stopped-Flow/CD with SFM-3 & MOS-400, Stopped-Flow/Fluorescence&Fluorescence Anisotropy with SFM-3 &  MOS-400 using the EMFA® method)

Kinetic Analysis of R67 Dihydrofolate Reductase Folding: From the Unfolded Monomer to the Native Tetramer
Christophe Bodenreider, Nicolas Kellershohn, Michel E. Goldberg, and Annick Méjean
Biochemistry ; 2002; 41(50); 14988-14999.
(SFM-300 + MOS components + Jobin-Yvon CD6)

Role of individual disulfide bonds in hen lysozyme early folding steps Valérie Guez, Pascale Roux, Amiel Navon and Michel E. Goldberg Protein Science (2002), 11:1136-1151
(SFM-300 + MOS components + Jobin-Yvon CD6)

Immunochemical pulsed-labeling characterization of intermediates during hen lysozyme oxidative folding Nicole M. Jarrett1, Lisa Djavadi-Ohaniance, Richard C. Willson, Hideki Tachibana and Michel E. Goldberg
Protein Science (2002), 11:2584-2595
(SFM-300 + MOS components + Jobin-Yvon CD6)

Kinetic Characterization of the pH-Dependent Oligomerization of R67 Dihydrofolate Reductase
Mejean, A.; Bodenreider, C.; Schuerer, K.; Goldberg, M. E.
Biochemistry ; 2001; 40(27); 8169-8179
(SFM-300 + MOS components + Jobin-Yvon CD6)

Detection of Two Partially Structured Species in the Folding Process of the Amyloidogenic Protein 2-Microglobulin
Fabrizio Chiti, Palma Mangione, Alessia Andreola, Sofia Giorgetti, Massimo Stefani, Christopher M. Dobson, Vittorio Bellotti, Niccolò Taddei
J.Mol.Biol. 2001, 307, 379-391
(SFM-300/ MOS-400 Fluo / CD / double Jump)

Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype B.
Do-Hyung Kim, Gyu Hyun Nam, Do Soo Jang, Sunggoo Yun, Gildon Choi, Hee Cheon Lee and Kwan Yong Choi
Protein Science (2001), 10:741-752
(SFM-400 + MOS-400/CD)

Equilibrium and Kinetic Analysis of Folding of Ketosteroid Isomerase from Comamonas testosteroni
Do-Hyung Kim, Do Soo Jang, Gyu Hyun Nam, Sunggoo Yun, Jae Hyun Cho, Gildon Choi, Hee Cheon Lee, and Kwan Yong Choi*
Biochemistry; 2000; 39(42); 13084-13092.
(SFM-4/QS, CD + fluorescence)

The Greek Key Protein Apo-pseudoazurin Folds Through an Obligate On-pathway Intermediate
Andrew P. Capaldi1, Stuart J. Ferguson2, Sheena E. Radford1
J. Mol. Biol. 286, 1621-1632
(SFM-3 + Jasco J-715 CD, CD)

Absence of stable intermediates on the folding pathway of barnase Takei, L.,Chu, RA, Bai, YW
PNAS 97 (20) 10796-10801 (2000)
(SFM-400 + MOS-400, CD + fluorescence)

Equilibrium and Kinetic Analysis of Folding of Ketosteroid Isomerase from Comamonas testosteroni
Do-Hyung Kim,Do Soo Jang, Gyu Hyun Nam,Sunggoo Yun, Jae Hyun Cho,Gildon Choi, Hee Cheon Lee, and Kwan Yong Choi
Biochemistry 2000, 39, 13084-13092
(SFM-400 + MOS-420/CD)

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
Jose C. Martínez & Luis Serrano
Nature Structural Biology, 1999 Volume 6 pp 1010 – 1016
(SFM-3)

Experiment and theory highlight role of native state topology in SH3 folding
David S. Riddle, Viara P. Grantcharova1, Jed V. Santiago, Eric Alm, Ingo Ruczinski & David Baker
Nature Structural Biology 1999 Volume 6 11 pp 1016 – 1024
(SFM-4)

Identifying the Site of Initial Tertiary Structure Disruption during Apomyoglobin Unfolding
Zhaoyang Feng, Jeung-Hoi Ha, and Stewart N. Loh
Biochemistry, 38 , 14433 -14439, 1999.
(SFM-4/QS)

Molecular Dissection of the Folding Mechanism of the R Subunit of Tryptophan Synthase: An Amino-Terminal Autonomous Folding Unit Controls Several Rate-Limiting Steps in the Folding of a Single Domain Protein
Jill A. Zitzewitz and C. Robert Matthews
Biochemistry 1999, 38, 10205-10214
(Fluorescence & CD with SFM-3 + Aviv CD + MOS-200)

Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants
Denis Canet, Margaret Sunde, Alexander M. Last, Andrew Miranker, Andrew Spencer, Carol V. Robinson, and Christopher M. Dobson
Biochemistry, 38 (20), 6419 -6427, 1999
(Fluorescence & CD with SFM-4)

R-Lytic Protease Precursor: Characterization of a Structured Folding Intermediate
D. Eric Anderson, Reuben J. Peters, Barry Wilk, and David A. Agard.
Biochemistry 1999, 38, 4728-4735
(CD with SFM-4/S + Jasco and SFM-4/Q)

Acceleration of the folding of acylphosphatase by stabilization of local secondary structure Fabrizio Chiti, Niccolo’ Taddei, Paul Webster, Daizo Hamada, Tania Fiaschi, Giampietro Ramponi & Christopher M. Dobson.
Nature Structural Biology 1999, Vol. 6, 293 – 397
(SFM + MOS-400)

Folding Mechanism of the alpha-Subunit of Tryptophan Synthase, an alpha/beta Barrel Protein: Global Analysis Highlights the Interconversion of Multiple Native, Intermediate, and Unfolded Forms through Parallel Channels
Osman Bilsel, Jill A. Zitzewitz, Katherine E. Bowers, and C. Robert Matthews.
Biochemistry 1999, 38, 1018-1029
(CD with SFM-3 + Aviv CD)

Initial hydrophobic collapse is not necessary for folding RNase A
Angela Nöppert, Klaus Gast, Dietrich Zirwer and Gregor Damaschun.
Folding & Design 1998, 3:213-221
(CD with SFM-3 + Jasco J-720 and Light scattering)

Probing the folding pathway of a -clam protein with single-tryptophan constructs
Patricia L Clark, Benjamin F Weston, Lila M Gierasch.
Folding & Design 1998, 3:401-412
(http://www.biomednet.com/library/abstract/JFAD.fd3510)
(Fluorescence with SFM-4 + PTI and CD with SFM-4 + Jasco J-715)

Mechanism of Folding of the Dimeric Core Domain of Escherichia coli Trp Repressor: A Nearly Diffusion-Limited Reaction Leads to the Formation of an On-Pathway Dimeric Intermediate
Lisa M. Gloss and C. Robert Matthews.
Biochemistry, 1998, 37, 15990-15999
(Fluorescence + CD with SFM + MOS + Aviv CD)

The Role of Ligand Binding in the Kinetic Folding Mechanism of Human p21 H-ras Protein
Jing Zhang and C. Robert Matthews
Biochemistry 1998, 37, 14891-14899
(SFM-3 + Aviv62DS spectrometer)

The burst phase in ribonuclease A folding and solvent dependence of the unfolded state Phoebe X. Qi1
Tobin R. Sosnick & S. Walter Englander.
Nature Structural Biology 1998 Volume 5 Number 10 pp 882 – 884
(FoldingCD with SFM-4 + Jasco 715)

Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding
Alex Kentsis and Tobin R. Sosnick
Biochemistry 1998, 37, 14613-14622 
(Fluorescence + CD with SFM-3 + SFM-4 + MOS-200 + Jasco)

Proline Isomerization-Independent Accumulation of an Early Intermediate and Heterogeneity of the Folding Pathways of a Mixed R/â Protein, Escherichia coli Thioredoxin
Roxana E. Georgescu, Jian-Hua Li, Michel E. Goldberg, Maria Luisa Tasayco, and Alain F. Chaffotte
Biochemistry 1998, 37, 10286-10297

Multiple Kinetic Intermediates Accumulate during the Unfolding of Horse Cytochrome c in the Oxidized State
Abani K. Bhuyan and Jayant B. Udgaonkar.
Biochemistry 1998, 37, 9147-9155
(http://pubs.acs.org/subscribe/journals/bichaw/jtoc.cgi?bichaw/37/25) note

Kinetic mechanism of luciferase subunit folding and assembly
AC Clark, SW Raso, JF Sinclair, MM Ziegler, AF Chaffotte, TO Baldwin.
Biochemistry, 1997, Vol 36, Iss 7, pp 1891-1899

Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L
ML Scalley, Q Yi, HD Gu, A McCormack, JR Yates, D Baker
Biochemistry, 1997, Vol 36, Iss 11, pp 3373-3382

Initial loss of secondary structure in the unfolding of barstar
Nath, U., Agashe, VR. and Udgaonkar, JB.
(1996) Nature Structural Biology, 3, 920-923

CD evidence for the presence of burst phase intermediates on the conformational folding pathway od ribonuclease
A. Houry WA, Rothwarf DM, Scheraga HA
(1996) Biochemistry, 35, 10125-10133

Folding of a four-helix bundle : studies of acyl-coenzyme A binding protein
Kragelund, BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM
(1995) Biochemistry, 34, 7217-7224

Understanding how proteins fold: the lysozyme story so far
Dobson, C.M., Evans, P.A. and Radford, S.E.
(1994) TIBS, 19, january

The refolding of human lysozyme: a comparaison with the structurally homologous hen lysozyme
Hooke, S.D., Radford, S.E. and Dobson, C.M.
(1994) Biochemistry, 33, 5867-5876

The barriers in protein folding
Sosnick, T.R., Mayne, L., Hiller, R. and Englander, S.W.
(1994) Nature Structural Biology 1, 149-155.

Tertiary interactions in the folding pathway of Hen lysozyme: kinetic studies using fluorescent probes
Itzhaki, L.S., Evans, P.A., Dobson, C.M. and Radford, S. E.
(1994) Biochemistry, 33, 5212-5220

Kinetic consequences of the removal of a disulfide bridge on the folding of Hen lysozyme
Eyles, S.J., Radford, S.E., Robinson, C.V. and Dobson, C.M.
(1994) Biochemistry, 33, 13038-13048

Kinetic characterization of the chemotactic protein from E. Coli, Che Y. Kinetic analysis of the inverse hydrophobic effect.
Munoz, V., Lopez, E.M., Jager, M. and Serrano, L.
(1994) Biochemistry, 33, 5858-5866

Structure and Stability of an Early Folding Intermediate of E-Coli TR Aprorepressor Measured by Far UV-CD and ANS Binding.
Mann, C. and Matthews, C.R.
(1993) Biochemistry, V.32, 5282-5290.

Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin
Jennings, P.A. and Wright, P.E.
(1993) Science, 262, 892-896.

Early Steps in Cytochromec Folding Observed by Time-Resolved Circular Dichroism and Fluorescence Spectroscopy.
Elove, G.A., ChafFotte, A.F., Roder, H., and Goldberg, M.E.
(1992), Biochemistry, 31, 6876-6883.

A Possible Initial Folding Intermediate: The C-Terminal Proteolytic Domain on Tryptophan Synthase B Chains Folds in Less than 4 Milliseconds into a Condense State with Non-native-like secondary Structure.
Chaffotte, A.F., Cadieux, C., Guillou, Y., Goldberg, M.E.
(1992) Biochemistry, 31, 4303-4308.

Kinetic Resolution of Peptide Bond and Side Chain Far-UV Circular Dichroism during the Folding of Hen Egg White Lysozyme.
Chaffotte, A.F., Guillou, Y., Goldberg, M.E.
(1992) Biochemistry, 31, 9695-9702.

The Folding of an Enzyme: IV. Structure of an Intermediaite in the Refolding of Barnase Analysed by a Protein Engineering Procedure
Matouschek, A., Serrano, L. and Fersht, A.
(1992) J. Mol. Biol. 224, 819-835.

Renaturation of guanidine-unfolded tryptophan synthase by multi-mixing stopped-flow dilution in D,O.
Blond-Elguindi, S., Friguet, B. and Goldberg, M.E.
(1988) FEBS Lett. 241, 251-256.

TOP 

Stopped-flow (cryo)

Mechanistic Information from Low-Temperature Rapid-Scan and NMR Measurements on the Protonation and Subsequent Reductive Elimination Reaction of a (Diimine)platinum(II) Dimethyl Complex
Bror J. Wik, Ivana Ivanovic-Burmazovic, Mats Tilset,* and Rudi van Eldik
Inorg. Chem., 45 (9), 3613 -3621, 2006
(cryoSFM-20+DAD)

TOP 

Stopped-flow (time resolved fluorescence)

Structural kinetics of myosin by transient time-resolved FRET
Yuri E. Nesmelov, Roman V. Agafonov, Igor V. Negrashov, Sarah E. Blakely, Margaret A. Titus, and David D. Thomas PNAS,
February 1, 2011, vol. 108, no. 5 (1891-1896)
(SFM-20/S + pulse laser coupling)

Hg2+-Reactive Double Hydrophilic Block Copolymer Assemblies as Novel Multifunctional Fluorescent Probes with Improved Performance
Jinming Hu, Changhua Li and Shiyong Liu Langmuir,
2010, 26 (2), pp 724–729
(SFM-300 + MOS-250)

Kinetics of Complex Formation between DNA and Cationically Charged Cylindrical Brush Polymers Observed by Stopped Flow Light Scattering
Frauke Kuehn, Karl Fischer, Manfred Schmidt
Macromolecular Rapid Communications, 2009, Volume 30 Issue 17, Pages 1470 – 1476
(SFM-300 I Light scattering)

RecQ Helicase-catalyzed DNA Unwinding Detected by Fluorescence Resonance Energy Transfer
Xing-Dong ZHANG, Shuo-Xing DOU, Ping XIE, Peng-Ye WANG, and Xu Guang
XI1 Acta Biochim Biophys Sin 2005,37:593-600
(SFM-400+MOS-450/AF-CD | Stopped-flow + FRET fluorescence)

Mapping the Cytochrome c Folding Landscape
Julia G. Lyubovitsky, Harry B. Gray,* and Jay R. Winkler*
J. AM. CHEM. SOC. 2002, 124, 5481-5485.
(http://pubs.acs.org/cgi-bin/abstract.cgi/jacsat/2002/124/i19/abs/ja017399r.html)  note 
(SFM-4 : double kinetics fluorescence lifetime)

Time-resolved fluorescence studies of the protein folding process: new instrumentation, analysis and experimental approaches.
Beechem, J.M., James, E. and Brand, L.
(1990) In: Time-resolved laser spectroscopy in biochemistry. SPIE proceedings series Vol. 1204, pp 685-698.

TOP 

Stopped-flow (fluorescence anisotropy)

Fluorometric assays for characterizing DNA helicases
Shuo-Xing Dou, Xu Guang Xi Methods, 2010: Volume 51, Issue 3, July 2010, Pages 295-302
(SFM-400 + MOS-450AF/CD)

Escherichia coli RecQ Is a Rapid, Efficient, and Monomeric Helicase
Xing-Dong Zhang, Ping Xie, Peng-Ye Wang, and Xu Guang Xi
J. Biol. Chem., Vol. 281, Issue 18, 12655-12663, May 5, 2006
(SFM-400 + MOS-450/AF-CD | Stopped-flow+ fluorescence anisotropy)

Kinetic and Structural Characterization of Adsorption-induced Unfolding of Bovine Þ-Lactalbumin
Maarten F. M. Engel, Carlo P. M. van Mierlo, and Antonie J. W. G. Visser
J. Biol. Chem., Mar 2002; 277: 10922 – 10930.
(http://www.jbc.org/cgi/content/abstract/277/13/10922)  note 
(SFM-400)

Characterization of Single-Tryptophan Mutants of Histidine-Containing Phosphocarrier Protein: Evidence for Local Rearrangements during Folding from High Concentrations of Denaturant
Azuaga, A. I.; Canet, D.; Smeenk, G.; Berends, R.; Titgemeijer, F.; Duurkens, R.; Mateo, P. L.; Scheek, R. M.; Robillard, G. T.; Dobson, C. M.; van Nuland, N. A. J.;
Biochemistry ; (Article); 2003; 42(17); 4883-4895.
(http://pubs.acs.org/cgi-bin/abstract.cgi/bichaw/2003/42/i17/abs/bi027182p.html) note
(Stopped-Flow/CD with SFM-3 & MOS-400, Stopped-Flow/Fluorescence&Fluorescence Anisotropy with SFM-3 &  MOS-400 using the EMFA® method)

New method for anisotropy measurement High-Sensitivity Fluorescence Anisotropy Detection of Protein-Folding Events: Application to alpha-Lactalbumin
Denis Canet, Klaus Doering, Christopher M. Dobson, and Yves Dupont
Biophys. J. 2001 80: 1996-2003
(http://www.biophysj.org/cgi/reprint/80/4/1996.pdf) note

Time-Resolved Fluorescence Anisotropy Study of the Refolding Reaction of the -Subunit of Tryptophan Synthase Reveals Nonmonotonic Behavior of the Rotational Correlation Time
Osman Bilsel, Li Yang, Jill A. Zitzewitz, Joseph M. Beechem, and C. Robert Matthews
Biochemistry 1999, 38 (13), 4177 -4187
(SFM-3)

Stopped-Flow Fluorescence Study of Precatalytic Primer Strand Base-Unstacking Transitions in the Exonuclease Cleft of Bacteriophage T4 DNA Polymerase
Michael R. Otto, Linda B. Bloom, Myron F. Goodman, and Joseph M. Beechem
Biochemistry 1998, 37, 10156-10163

Distinct action of cis and trans ATP within the double ring of the chaperonin GroEL
Rye HS, Burston SG, Fenton WA, Beechem JM, Zhaohui Xu, Sigler PB and Horwich. AL
Nature 388, 792-798 (1997)

Sequential domain unfolding in phosphoglycerate kinase : fluorescence anisotropy stopped-flow kinetics of sevral tryptophan mutants
Beechem, JM, Sherman MA, Mas MT
(1995) Biochemistry, 34, 13943-13948

Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments
Otto MR, Lillo MP, Beechem, JM
(1994) Biophysical J. 67, 2511-2521

TOP 

Stopped-flow (diode array)

Evaluation of proton activity in microemulsions by a kinetic probe
Indalecio A. Penacoba, Begona Garcia, Ana M. Navarro, F. Javier Hoyuelos, Jose M. Leal
Journal of Colloid and Interface Science, Volume 352, Issue 2, 15 December 2010, Pages 465-469
(http://www.sciencedirect.com/science/article/B6WHR-511G1SH-5/2/3e0ee3e607852996a6f0b207b7f5e7f6)
(SFM-400 + DAD)

Growth Mechanisms in Nanocrystalline Lead Sulfide by Stopped-Flow Kinetic Analysis
Allison L. Brazeau and Nathan D. Jones Department of Chemistry, The University of Western Ontario, London, Ontario, Canada, N6A 5B7
J. Phys. Chem. C, 2009, 113 (47), pp 20246–20251
(SFM-300 + DAD UV-VIS)

Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols
Jeremiah Feducia, Rania Dumarieh, Lauren B. G. Gilvey, Tatyana Smirnova, Stefan Franzen, and Reza A. Ghiladi Department of Chemistry, North Carolina State UniVersity, Raleigh, North Carolina 27695
Biochemistry 2009, 48, 995–1005 (SFM-400 + DAD)

Characterization of human D-amino acid oxidase
Gianluca Molla, Silvia Sacchi, Mariagrazia Bernasconi, Mirella S. Pilone, Kiyoshi Fukui, Loredano Pollegioni
FEBS Letters 580 (2006) 2358–2364
(http://www.dbsm.uninsubria.it/biochim/publications/papers/2006b_molla.pdf) note
(SFM-300+DAD)

Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study
Chantal CAPEILLERE-BLANDIN, Delphine MATHIEU and Daniel MANSUY
Biochem. J. (2005) 392, 583–587
(http://www.biochemj.org/bj/392/0583/3920583.pdf) note
(SFM-3 + Diode array)

Multistate reaction kinetics of 6-hydroxy-4-(dimethylamino)flavylium driven by pH. A stopped-flow study
César A. T. Laia, A. Jorge Parola, Filipe Folgosa and Fernando Pina
Org. Biomol. Chem., 2007, 5, 69 – 77
(SFM-300 + DAD | Stopped-Flow diode array)

In situ investigation of the oxidative addition in homogeneous Pd catalysts by synchronised time resolved UV-Vis/EXAFS
Gemma Guilera*a, Mark A. Newtona, Charlene Pollia, Sakura Pascarellia, Meritxell Guinób and King Kuog (Mimi) Hii*b
a) European Synchrotron Radiation Facility (ESRF, ID24), P.O. Box 220, 38043 Grenoble Cedex, France. E-mail: guilera@esrf.fr; Fax: +33 (0)4 7688 2784; Tel: +33 (0)4 3888 1930
b) Department of Chemistry, Imperial College London, Exhibition Road, South Kensington, UK SW7 2AZ. E-mail: mimi.hii@imperial.ac.uk; Fax: +44 (0)20 7594 5804; Tel: +44 (0)20 7594 1142
Chem. Commun., 2006, DOI: 10.1039/b606772g
(SFM-300+Diode array+EXAFS)

Mechanistic Information from Low-Temperature Rapid-Scan and NMR Measurements on the Protonation and Subsequent Reductive Elimination Reaction of a (Diimine)platinum(II) Dimethyl Complex
Bror J. Wik, Ivana Ivanovic-Burmazovic, Mats Tilset,* and Rudi van Eldik
Inorg. Chem., 45 (9), 3613 -3621, 2006
(cryoSFM-20+DAD)

Evidence of Two Distinct Oxygen Complexes of Reduced Endothelial Nitric Oxide Synthase
Stéphane Marchal, Morten Sørlie, K. Kristoffer Andersson, Bernd Mayer, and Reinhard Lange
J. Biol. Chem., Vol. 279, Issue 19, 19824-19831, May 7, 2004
(SFM-300+DAD+MOS-200)

Two coupled photochromic systems of 3′,4′-(methylendioxy)flavilium : kinetic and thermodynamic characterisation
D.Fernàndez, F.Folgosa, A.J.Parola, F.Pina
New.J.Chem., 2004, 28, 1221-11226
(SFM-300 + diode array)

Acid-base behavior of organopalladium complexes [Pd(CNN)R]BF4
M.S.Munoz, B.Garcia, S.Ibeas, F.J.Hoyuelos,I.Penacoba, A.M.Navarro,J.M.Leal
New.J.Chem., 2004, 28, 1450-1456
(SFM-300 + diode array)

Ozonolysis of vinyl compounds, CH2=CH-X, in aqueous solution – the chemistries of ensuing formyl compounds and hydrolysis
Leitzke A, Flyunt R, Theruvathu JA, von Sonntag C.
2003. Org. Biomol. Chem.: 4, 1012-1019
(SFM + diode array + conductimetry)

Kinetic mechanisms of glycine oxidase from Bacillus subtilis
Gianluca Molla, Laura Motteran, Viviana Job, Mirella S. Pilone and Loredano Pollegioni
Eur. J. Biochem. 270, 1474-1482 (2003)
(http://www.ejbiochem.org/cgi/content/abstract/270/7/1474) note
(SFM + diode array and operation in anaerobic conditions)

Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase A site-directed mutagenesis study
Angelo Boselli, Silvia Sacchi, Viviana Job, Mirella S. Pilone and Loredano Pollegioni
Eur. J. 269, 4762-4771 (2002)
(http://www.ejbiochem.org/cgi/content/abstract/269/19/4762) note
(SFM + diode array and operation in anaerobic conditions)

The reaction of thymine and thymidine with ozone
Flyunt R, Theruvathu JA, Leitzke A, von Sonntag C.
2002. J. Chem. Soc., Perkin Trans.: 2, 1572-1582
(SFM + diode array + conductimetry)

Kinetics of aqueous acid hydrolysis of Iron(III) 5-substituted-8-hydroxyquinoline complexes : mechanistic implications
H.Boukhalfa, F.Thomas, G.Serratrice, C.Beguin
Inorganic reaction Mechanism, vol3, (2002), 153-172
(SFM + diode array)

Hydrolytic removal of chlorinated products from the oxidative free-radical-induced degradation of chloroethylenes: acid chlorides and chlorinated acetic acids
Prager L, Dowideit P, Langguth H, Schuchmann HP, von Sonntag C.
2001. J. Chem. Soc., Perkin Trans.: 2, 1641-1647
(SFM + diode array + conductimetry)

Iron(III) complexation by new aminocarboxylate chelators-thermodynamic and kinetic studies
G.Serratrice, JB.Galey, E.Saint Aman, J.Dumats
Eur. J.Inorg.chem. 2001, 471-479
(SFM + diode array)

Biomimetic studies related to the azide-inhibited Cu,Zn superoxide dismutase
G. Serratrice, C. Beguin, P. Chautemps, C.Cogne, JL.Pierre
New J.Chem., 2001, 25, 696-699
(SFM + diode array)

‘Biosynthesis of Pteridines. Stopped-flow kinetic analysis of GTP Cyclohydrolase I’
A.Bracher, N. Schramek, A. Bacher
Biochemistry 2001, 40, 7896-7902
(SFM4/QS + Diode array)

Thermodynamic and kinetic studies of the sulfonated derivative of the iron chelator TRENCAM, an analog of enterobactin
F.Thomas, C.Beguin, JL.Pierre, G.Serratrice
Inorganica Chimica Acta 291 (1999) 148-157
(SFM + diode array)

Calcein as a fluorescent probe for ferric iron
F.Thomas,G.Serratrice, C.Beguin, E.Saint Aman, JL.Pierre,M.Fontecave, JP.Laulhère
Journal of Biological chemistry, vol.274, No19, 99 13375-13383,(1999)
(SFM + diode array)

Reaction of Ozone with ethylene and its methyl- and chlorine-substituted derivates in aqueous solution
Dowideit P, von Sonntag C.
1998. Environ. Sci. Technol.: 32, 1112-1119
(SFM + diode array + conductimetry)

O-TRENSOX, a New Tripodal Iron Chelator Based on 8-Hydroxyquinoline Subunits: Thermodynamic and Kinetic Studies
Guy Serratrice, Hakim Boukhalfa, Claude Béguin, Paul Baret, Catherine Caris, and Jean-Louis Pierre
Inorganic Chemistry, 36, 3898-3910 (1997)

Characterization of the Reaction Mechanism for Trypanosoma brucei Ornithine Decarboxylase by Multiwavelength Stopped-Flow Spectroscopy
Harold B. Brooks and Margaret A. Phillips*.
Biochemistry 1997, 36, 15147-15155

Non-hydrolytic decay of formyl chloride into CO and HCl in aqueous solution
Dowideit P, Mertens R, von Sonntag C.
1996. J. Am. Chem. Soc.: 118, 11288-11292
(SFM + diode array + conductimetry)

TOP 

Stopped-flow (synchrotron radiation)

Multitechnique Approach to Reveal the Mechanism of Copper(II)-Catalyzed Arylation Reactions
Moniek Tromp, Gino P. F. van Strijdonck, Sander S. van Berkel, Adri van den Hoogenband, Martinus C. Feiters,Bas de Bruin, Steven G. Fiddy,Ad M. J. van der Eerden, Jeroen A. van Bokhoven, Piet W. N. M. van Leeuwen, and Diederik C. Koningsberger
Organometallics 2010, 29, 3085–3097
(SFM-400 + ED-XAFS+simultaneous diode array)

Applications of stopped-flow in SAXS and SANS
Isabelle Grillo
Current Opinion in Colloid and Interface Science 14 (2009) 402-408
(SFM-300)

Local structure of reaction intermediates probed by time-x-ray absorption near edge structure spectroscopy
G. Smolentsev, G. Guilera, M. Tromp, S. Pascarelli, and A. V. Soldatov
THE JOURNAL OF CHEMICAL PHYSICS 130, 174508 (2009)
(SFM-300 + ED-EXAFS)

In situ investigation of the oxidative addition in homogeneous Pd catalysts by synchronised time resolved UV-Vis/EXAFS
Gemma Guilera*a, Mark A. Newtona, Charlene Pollia, Sakura Pascarellia, Meritxell Guinób and King Kuog (Mimi) Hii*b
a) European Synchrotron Radiation Facility (ESRF, ID24), P.O. Box 220, 38043 Grenoble Cedex, France. E-mail: guilera@esrf.fr; Fax: +33 (0)4 7688 2784; Tel: +33 (0)4 3888 1930
b) Department of Chemistry, Imperial College London, Exhibition Road, South Kensington, UK SW7 2AZ. E-mail: mimi.hii@imperial.ac.uk; Fax: +44 (0)20 7594 5804; Tel: +44 (0)20 7594 1142
Chem. Commun., 2006, DOI: 10.1039/b606772g
(SFM-300+Diode array+EXAFS)

Dynamics of structural transitions in amphiphilic systems monitored by scattering techniques
M. Gradzielski, I. Grillo, T. Narayanan
Prog Colloid Polym. Sci. (2004) 129: 32-39

Deactivation processes of homogeneous Pd catalysts using in situ time resolved spectroscopic techniques
Moniek Tromp , Jelle R. A. Sietsma , Jeroen A. van Bokhoven , Gino P. F. van Strijdonck , Richard J. van Haaren , Ad M. J. van der Eerden , Piet W. N. M. van Leeuwen and Diek C. Koningsberger
Chem. Commun., 2003, (1), 128 – 129.
(SFM-4 + ED-XAFS)

Time-resolved scattering investigations of brome mosaic virus microcrystals appearance
M. Casselyn, S. Finet, A. Tardieu and H. Delacroix
Acta Cryst. (2002). D58, 1568-1570
(SFM-3 + small angle X-ray scattering)

Application of stopped flow techniques and energy dispersive EXAFS for investigation of the reactions of transition metal complexes in solution: Activation of nickel-diketonates to form homogeneous catalysts, electron transfer reactions involving iron(III) and oxidative addition to iridium(I)
M. Basyaruddin B. Abdul Rahman , Peter R. Bolton , John Evans , Andrew J. Dent , Ian Harvey and Sofia Diaz-Moreno
Faraday Discuss., 2002, (Advance Article) First published on the web 16th july 2002

Energy dispersive X-ray absorption spectroscopy; a tool for time resolved structural studies of chemical reactions in solution
Sofia Diaz-Moreno in “From Semiconductor to Proteins : Beyond the Average Structure”
SJL Billinge & MF Thorpe Ed., Kluwer Academic/Plenum Publishers
(http://www.esrf.fr/info/science/newsletter/oct99/DOSEXP/EXP7.htm)  note 
March 2002

Fast Kinetics Study of Mesoporous Material Growth by Small-angle X-ray Scattering
F. Né, F. Testard, Th. Zemb and J-M. Petit
ESRF Newsletter Oct. 1999
(http://www.esrf.fr/info/science/newsletter/oct99/DOSEXP/EXP7.htm)

TOP 

Stopped-flow (small angle neutron scattering)

Applications of stopped-flow in SAXS and SANS
Isabelle Grillo
Current Opinion in Colloid and Interface Science 14 (2009) 402-408
(SFM-300)

Dynamics of structural transitions in amphiphilic systems monitored by scattering techniques
M. Gradzielski, I. Grillo, T. Narayanan
Prog Colloid Polym. Sci. (2004) 129: 32-39

How does ZrO2/surfactant mesophase nucleate? Formation mechanism
F. Né, F. Testard, Th. Zemb, I. Grillo
Langmuir (2003), 19(20), 8503-8510
(SFM-3 & ILL neutron beam)

Formation and growth of anionic vesicles followed by small angle neutron scattering
I. Grillo, E.I. Kats, A.R. Muratov
Langmuir (2003), 19 (11) 4573-4581
(SFM-3 & ILL neutron beam)

Formation and growth of anionic vesicles followed by small angle neutron scattering.
Grillo I, Kats E, Muratov AR.
Langmuir 2003;19:4573-4581
(SFM300/S)

How does ZrO2/surfactant mesophase nucleate? Formation mechanism.
Né F, Testard F, Zemb Th, Grillo I.
Langmuir 2003;19:8503-8510
(SFM300/S)

Monomer-aggregate exchange rates in dialkyl chain cationic-nonionic surfactant mixtures.
Tucker I., Penfold J., Thomas R.K., Grillo I.
Langmuir (2009), 25, 2661-2666
(SFM300/S)

Time-resolved small-angle neutron scattering as a lamellar phase evolves into a microemulsion
Tabor R.F., Eastoe J., Grillo I.
Soft Matter(2009), 5, 2125-2129
(SFM300/S)

Applications of stopped-flow in SAXS and SANS
Grillo I.
Current Opinion in Colloids and Interface Science (2009), 6, 402-408
(SFM300/S)

Mesodynamics: watching vesicle formation in situ by small-angle neutron scattering
Bressel K., Muthig M., Prevost S., Grillo I., Gradzielski M.
Colloid and Polymer Sc (2010) 288, 827-840
(SFM300/S)

Dynamics of Formation of Vesicles Studied by Highly Time-resolved Stopped-flow Experiments
Barth A.; Grillo I.; Gradzielski M.
Tenside surfactant detergents (2010) 47, 300-306
(SFM300/S)

Equilibrium Chain Exchange Kinetics of Diblock Copolymer Micelles: Effect of Morphology
Lund R., Willner L., Pipich V., Grillo I., Lindner P., Colmenero J., Richter D.
Macromolecules (2011) 44, 6145-6154
(SFM300/S)

Kinetics of the Formation of 2D-Hexagonal Silica Nanostructured Materials by Nonionic Block Copolymer Templating in Solution
Manet S., Schmitt J., Impéror-Clerc M., Zholobenko V., Durand D., Oliveira C.L.P., Pedersen J.S., Gervais C., Baccile N., Babonneau F., Grillo I., Meneau F., Rochas C.
J. Phys. Chem. B (2011) 115, 11330–11344
(SFM300/S)

Growth of mesoporous silica nanoparticles monitored by time-resolved small-angle neutron scattering
Hollamby M.J., Borisova P., Eastoe J., Grillo I., Shchukin D.
Langmuir (2012) 28, 4425-4433
(SFM300/S)

Kinetics of collapse transition and cluster formation in a thermoresponsive micellar solution of P(S-b-NIPAM-b-S) induced by a temperature jump
Adelsberger J., Metwalli E., Diethert D., Grillo I., Bivigou-Koumba A.M, Laschewsky A.,, Müller-Buschbaum and P., Papadakis C.M.
Macromol. Rapid Commun. (2012) 33, 254-259
(SFM300/S)

Kinetics of aggregation in micellar solutions of thermoresponsive triblock copolymers – influence of concentration, start and target temperatures
Adelsberger J., Grillo I., Kulkarni A., Sharp M., Bivigou-Koumba A. M., Laschewsky A., Müller-Buschbaum P., Papadakis C. M.,
Soft Matter (2013) 9, 1685-1699
(SFM300/S)

TOP 

Stopped-flow (conductimetry)

Reaction kinetics of CO2 in aqueous methyldiethanolamine solutions using the stopped-flow technique
Kierzkowska-Pawlak, Hanna; Siemieniec, Marta; Chacuk, Andrzej
Chemical and Process Engineering, 2011, 33(1), 7-18
(SFM-20+MCS-200)

Reaction kinetics of carbon dioxide in aqueous diethanolamine solutions using the stopped-flow technique
Siemieniec, Marta; Kierzkowska-Pawlak, Hanna; Chacuk, Andrzej
ECOL CHEM ENG S. 2012;19(1):55-66
(SFM-20+MCS-200)

Ozonolysis of vinyl compounds, CH2=CH-X, in aqueous solution – the chemistries of ensuing formyl compounds and hydrolysis
Leitzke A, Flyunt R, Theruvathu JA, von Sonntag C.
2003. Org. Biomol. Chem.: 4, 1012-1019
(SFM + diode array + conductimetry)

The reaction of thymine and thymidine with ozone
Flyunt R, Theruvathu JA, Leitzke A, von Sonntag C.
2002. J. Chem. Soc., Perkin Trans.: 2, 1572-1582
(SFM + diode array + conductimetry)

Hydrolytic removal of chlorinated products from the oxidative free-radical-induced degradation of chloroethylenes: acid chlorides and chlorinated acetic acids
Prager L, Dowideit P, Langguth H, Schuchmann HP, von Sonntag C.
2001. J. Chem. Soc., Perkin Trans.: 2, 1641-1647
(SFM + diode array + conductimetry)

Reaction of Ozone with ethylene and its methyl- and chlorine-substituted derivates in aqueous solution
Dowideit P, von Sonntag C.
1998. Environ. Sci. Technol.: 32, 1112-1119
(SFM + diode array + conductimetry)

Non-hydrolytic decay of formyl chloride into CO and HCl in aqueous solution
Dowideit P, Mertens R, von Sonntag C.
1996. J. Am. Chem. Soc.: 118, 11288-11292
(SFM + diode array + conductimetry)

TOP 

Stopped-flow (anaerobic conditions)

Biochemical Characterization and Ligand Binding Properties of Neuroglobin, a Novel Member of the Globin Family
Sylvia Dewilde, Laurent Kiger, Thorsten Burmester,Thomas Hankeln, Veronique Baudin-Creuza, Tony Aerts, Michael C. Marden, Roland Caubergs, and Luc Moens
J. Biol. Chem., Vol. 276, Issue 42, 38949-38955, October 19, 2001
(http://www.jbc.org/cgi/content/full/276/42/38949#SEC1) note
(SFM-3 + MOS-200)

Characterization of human D-amino acid oxidase
Gianluca Molla, Silvia Sacchi, Mariagrazia Bernasconi, Mirella S. Pilone, Kiyoshi Fukui, Loredano Pollegioni
FEBS Letters 580 (2006) 2358–2364
(http://www.dbsm.uninsubria.it/biochim/publications/papers/2006b_molla.pdf) note
(SFM-300+DAD)

Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study
Chantal CAPEILLERE-BLANDIN, Delphine MATHIEU and Daniel MANSUY
Biochem. J. (2005) 392, 583–587
(http://www.biochemj.org/bj/392/0583/3920583.pdf) note
(SFM-3 + Diode array)

Evidence of Two Distinct Oxygen Complexes of Reduced Endothelial Nitric Oxide Synthase
Stéphane Marchal, Morten Sørlie, K. Kristoffer Andersson, Bernd Mayer, and Reinhard Lange
J. Biol. Chem., Vol. 279, Issue 19, 19824-19831, May 7, 2004
(SFM-300+DAD+MOS-200)

Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.
Whittaker MM, Whittaker JW
J Biol Chem. 2003 Jun 13;278(24): 22090-101.
(SFM-300 in anaerobic conditions)

Kinetic mechanisms of glycine oxidase from Bacillus subtilis
Gianluca Molla, Laura Motteran, Viviana Job, Mirella S. Pilone and Loredano Pollegioni
Eur. J. Biochem. 270, 1474-1482 (2003)
(http://www.ejbiochem.org/cgi/content/abstract/270/7/1474) note
(SFM + diode array and operation in anaerobic conditions)

Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase A site-directed mutagenesis study
Angelo Boselli, Silvia Sacchi, Viviana Job, Mirella S. Pilone and Loredano Pollegioni
Eur. J. 269, 4762-4771 (2002)
(http://www.ejbiochem.org/cgi/content/abstract/269/19/4762) note
(SFM + diode array and operation in anaerobic conditions)

TOP 

Stopped-flow (FT-IR/IR detection)

A Millisecond Infrared Stopped-Flow Apparatus
Jia Tang and Feng Gai
Applied Spectroscopy, Vol. 60, Issue 12, pp. 1477-1481
(SFM-300 + FT-IR accessory)

TOP 

Stopped-flow (mT jump)

Comparative Study of Temperature-Induced Association of Cyclic and Linear Poly(N-isopropylacrylamide) Chains in Dilute Solutions by Laser Light Scattering and Stopped-Flow Temperature Jump
Jing Ye, Jian Xu, Jinming Hu, Xiaofeng Wang, Guangzhao Zhang, Shiyong Liu, Chi Wu
Macromolecules, 2008, 41 (12), pp 4416–4422
(SFM300 + MOS250-mT jump)

Distinct Unfolding and Refolding Pathways of Ribonuclease A Revealed by Heating and Cooling Temperature Jumps
Joan Torrent, Stéphane Marchal , Marc Ribó , Maria Vilanova , Cédric Georges , Yves Dupont and Reinhard Lange
Biophysical Journal 94:4056-4065 (2008)
(SFM-300+mT-jump+MOS-200)

Micellization Kinetics of a Novel Multi-Responsive Double Hydrophilic Diblock Copolymer Studied by Stopped-Flow pH and Temperature Jump
Yanfeng Zhang, Tao Wu, Shiyong Liu
Macromol. Chem. Phys. 2007, 208, 2492–2501
(SFM-300+mT-jump+MOS-250)

TOP 

Stopped-flow (other applications)

Mixer coupled to EPR

An advanced EPR stopped-flow apparatus based on a dielectric ring resonator
Günter Lassmann, Peter Paul Schmidt and Wolfgang Lubitz
Journal of Magnetic Resonance, Volume 172 Issue 2 , February 2005, Pages 312-323

Reaction stop by filtration

Are the States That Occlude Rubidium Obligatory Intermediates of the Na/K-ATPase Reaction?
Sergio B. Kaufman, Rodolfo M. Gonzalez-Lebrero, Pablo J. Schwarzbaum, Jens G. Nørby, Patricio J. Garrahan, and Rolando C. Rossi
THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, pp. 20779-20790, 1999
(http://www.jbc.org/cgi/content/full/274/30/20779)  note

An attachment for non-destructive, Fast-Quenching of samples in rapid-mixing experiments.
Rossi, R. C., Kaufman, S. B., Gonzalez-Lebrero, R. M., Nørby, J. G., and Garrahan, P. J.
Anal. Biochem 270, 276-285 (1999)

Stopped-flow coupled to mass spectrometry

From Small-Molecule Reactions to Protein Folding: Studying Biochemical Kinetics by Stopped-Flow Electrospray Mass Spectrometry
Beata M. Kolakowski and Lars Konermann
Analytical Biochemistry 292, 107-114 (2001)
Researcher’s Web: http://publish.uwo.ca/~konerman/research.htm#SF_MS

TOP 

Spectrometers (fluorescence, light scattering, absorbance)The Formin Homology 1 Domain Modulates the Actin Nucleation and Bundling Activity of Arabidopsis FORMIN1
Alphée Michelot, Christophe Guérin, Shanjin Huang, Mathieu Ingouff, Stéphane Richard, Natalia Rodiuc, Christopher J. Staiger, and Laurent Blanchoin
Plant Cell. 2005 August; 17(8): 2296–2313
(MOS-450/AF-CD | slow kinetics fluorescence)

Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K+ Channels
Wei Zhou, Yan Qian, Kumud Kunjilwar, Paul J. Pfaffinger and Senyon Choe
Neuron, Volume 41, Issue 4 , 19 February 2004, Pages 573-586
(MOS-450/AF-CD | steady state AF+CD)

Steps towards Phage Display Libraries with an extended amino acid repertoire
M. Björklund, E. Koivonen
Letters in Drud Design and Discovery, 2004, 1, 163-167
(MOS-250 emission fluorescence)

Phosphorylation of the WASP-VCA Domain Increases Its Affinity for the Arp2/3 Complex and Enhances Actin Polymerization by WASP
Giles O.C. Cory, Rainer Cramer, Laurent Blanchoin, and Anne J. Ridley
Molecular Cell, Vol. 11, 1229–1239, May, 2003
(MOS-450, steady state or slow kinetics recordings)

Investigation of the Secondary DNA-binding Site of the Bacterial Recombinase RecA
Christophe Cazaux, Jean-Sébastien Blanchet, Delphine Dupuis, Giuseppe Villani, Martine Defais, and Neil P. Johnson
J Biol Chem 1998, 273, 28799-28804
(http://www.jbc.org/cgi/content/full/273/44/28799) note (steady state with MOS-400)

Interaction between Delta-subunits and Epsilon-subunits of Fl-ATPase from pig heart mitochondria. Circular dichroism and intrinsic fluorescence of purified and reconstituted Delta-epsilon-complex.
Penin, F., Deleage, G., Gagliardi, D., Roux, B. and Gautheron, D.C.
(1990) Biochemistry, 29, 9358-9364.

TOP 

Spectrometers (circular dichroism)

Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH
Hassan Al-Ali, Megan E. Rieger, Kenneth L. Seldeen, Thomas K. Harris, Amjad Farooq and Karoline J. Briegel
Biochemical and Biophysical Research Communications- Volume 391, Issue 1, 1 January 2010, Pages 1104-1109
(SFM-400 + MOS-450AF/CD)

Structural Characterization of Apomyoglobin Self-Associated Species in Aqueous Buffer and Urea Solution
Charles Chow , Nese Kurt *, Regina M. Murphy and Silvia Cavagnero
Biophysical Journal 90:298-309 (2006)
(MOS-450/AF-CD + SFM-400 | CD stopped-flow and CD steady state mode)

Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K+ Channels
Wei Zhou, Yan Qian, Kumud Kunjilwar, Paul J. Pfaffinger and Senyon Choe
Neuron, Volume 41, Issue 4 , 19 February 2004, Pages 573-586
(MOS-450/AF-CD | steady state AF+CD)

Amino Acids of the Bacterial Toxin SopE Involved in G Nucleotide Exchange on Cdc42
Markus C. Schlumberger <l >, Gretel Buchwald, Klaus Scheffzek , Alfred Wittinghofer , and Wolf-Dietrich Hardt
J. Biol. Chem., Vol. 278, Issue 29, 27149-27159, July 18, 2003
(SFM-20 + MOS-450 AF/CD | SF Fluorescence and steady state CD spectra)

Ellipticity changes of the sarcoplasmic reticulum Ca-ATPase induced by cation binding and phosphorylation.
Girardet, J.L. & Dupont, Y.
(1992) FEBS Lett., 296, 103-106.

TOP 

Spectrometers (fluorescence anisotropy)

DNA: REPLICATION REPAIR AND RECOMBINATION: Kinetic Mechanism for the Formation of the Presynaptic Complex of the Bacterial Recombinase RecA
Martine Defais, Emilie Phez, and Neil P. Johnson
J. Biol. Chem., Jan 2003; 278: 3545 – 3551
(http://www.jbc.org/cgi/content/abstract/278/6/3545)  note
(MOS-400, Steady state or slow kinetics recordings)

TOP 

Quench-Flow

The mechanism of addition of pyridoxal 5´-phosphate to Escherichia coli apo-serine hydroxymethyltransferase
Francesca MALERBA, Andrea BELLELLI, Alessandra GIORGI, Francesco BOSSA and Roberto CONTESTABILE
Biochem. J. (2007) 404 (477–485)
(QFM-400)

Cytochrome b5 Increases the Rate of Product Formation by Cytochrome P450 2B4 and Competes with Cytochrome P450 Reductase for a Binding Site on Cytochrome P450 2B4
Haoming Zhang, Sang-Choul Im, and Lucy Waskell
THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 282, NO. 41, pp. 29766–29776 ( 2007)
QFM-400 ( anaerobic conditions)

Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+ activated states of sarcoplasmic reticulum Ca2+ – ATPase
D.B.McIntosh, J.D.Clausen, D.G. Woolley, D.H.MacLennan, B.Vilsen, J.P.Andersen
Journal of biological Chemistry, vol.279, (2004)
QFM-5 (double mixing)

Glutamate-183 in the conserved TGES motif of domain A of sarcoplasmic reticulum Ca2+ – ATPase assists in catalysis of E2/E2P partial reactions
J.D.Clausen, B.Vilsen, D.B.McIntosh, A.P.Einholm, J.P. Andersen
PNAS, 2776-2781, march 2004, vol.101, n° 9
QFM-5 and SFM-400/Q (double mixing)

Importance of transmembrane segment M1 of the sarcoplasmic reticulum Ca2+-ATPase in Ca2+ occlusion and phosphoenzyme processing
A.P.Einholm, B.Vilsen, J.P.Andersen
Journal of biological Chemistry, vol.279, n°16, (2004), 15888-15896
QFM-5 and SFM-400/Q (double mixing)

Roles of Leu249, Lys252 and Leu253 in membrane segment M3 of sarcoplasmic reticulum Ca2+-ATPase in control of Ca2+ migration and Long-range intramolecular communication
J.D.Clausen, J.P.Andersen
Biochemistry (2003), 42, 2585-2594
QFM-5 and SFM-400/Q (double mixing)

Dissection of the functionnal differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of darier disease (SERCA2)mutants by steady-state and transient kinetic analysis
L.Dode, J.P.Andersen, N. Leslie, J.Dhitavat, B.Vilsen, A.Hovnanian
Journal of biological Chemistry, vol.278, n°48, (2003), 47877-47889
QFM-5 (double mixing)

Importance of conserved N-domain residues thr441, Glu442, lys515, Arg560, Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps
J.D.Clausen, D.B. McIntosh, B.Vilsen, D.G.Woolley, J.P. Andersen
Journal of biological Chemistry, vol.278, n°22, (2003), 20245-20258
QFM-5 (double mixing)

Importance of conserved Thr214 in domain A of the Na+, K+ – ATPase for stabilization of the phosphoryl state complex in E2P dephosphorylation
M. Toustrup-Jensen, B. Vilsen
Journal of biological Chemistry, vol.278, n°19, (2003), 11402-11410
QFM-5 (double mixing)

Functional consequences of alterations of Ile279, Ile283, Glu284, his285, Phe286, and His288 in the NH2-terminal part of the transmembrane helix M3 of the Na+, K+ – ATPase
M. Toustrup-Jensen, B. Vilsen
Journal of biological Chemistry, vol.278, n°40, (2003), 38653-38664
QFM-5 (double mixing)

Facile Variation of Reagent Concentrations in Rapid Quench Enzymology.
Sohn, J. and Rudolph, J. (2003)  Anal. Biochem. 312, 80-83
(QFM-400 microvolume Quench-Flow)

Catalytic Mechanism of the Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26.
Prokop, Z., Monincova, M., Chaloupkova, R., Klvana, M., Nagata, Y., Janssen, D.B., Damborsky, J.
2003: Journal of Biological Chemistry 278: 45094-45100.
(QFM-400 microvolume Quench-Flow & SFM-20+J-810 in Fluo)

The complex between a four-way DNA junction and T7 endonuclease 1
A.C.Déclaix, J.M.Fogg, A.D.J.Freeman, F. Coste, J.M.Hadden, S.E.V.Phillips and David M.J.Lilley
EMBO vol 22 no.6 pp 1398-1409 2003 
(QFM-400 microvolume Quench-Flow)

Dissection of the functionnal differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analysis
L.Dode, B.Vilsen, K. Van Baelen, F. Wuytack, J.D. Clausen, J.P.Andersen
Journal of biological Chemistry, vol.277, n°47, (2002), 45579-45591
QFM-5 (double mixing)

Importance of Glu282 in transmembrane segment M3 of the of the Na+,K+-ATPase for control of the cation interaction and conformational changes
M. Toustrup-Jensen, B. Vilsen
Journal of biological Chemistry, vol.277, n°41, (2002), 38607-38617
QFM-5 (double mixing)

Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I.
Hadden JM, Declais AC, Phillips SE, Lilley DM.
EMBO J 2002 Jul 1;21(13):3505-15
(QFM-400 microvolume Quench-Flow)

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
Denis Canet, Alexander M. Last, Paula Tito, Margaret Sunde, Andrew Spencer, David B. Archer, Christina Redfield, Carol V. Robinson & Christopher M. Dobson
Nature structural Biology (2002) vol 9, pp 308 – 315
(QFM-5 coupled to mass spectrometry)

Importance of transmembrane segment M3 of the sarcoplasmic reticulum Ca2+-ATPase for control of the gateway to the Ca2+ sites
J.P. Andersen, T.Lykke-Moller Sorensen, K. Povlsen, b. Vilsen
Journal of biological Chemistry, vol.276, n°26, (2001), 23312-23321
QFM-5 (double mixing)

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity
J.D. Clausen, D.B. McIntosh, D.G.Woolley, J.P.Andersen
Journal of biological Chemistry, vol.276, n°38, (2001), 35741-35750
QFM-5 (double mixing)

Mutational effects on conformational changes of the dephospho-and phospho-forms of the Na+,K+-ATPase
M. Toustrup-Jensen, M. Hauge, B. Vilsen
Biochemistry (2001), 40, 5521-5532
QFM-5 (double mixing)

Importance of stalk segment S5 for Intramolecular communication in the sarcoplasmic Ca2+-ATPase
Thomas Lykke-Moller Sorensen, Jens Peter Andersen
Journal of biological Chemistry, vol.275, n°37, (2000), 28594-28961
QFM-5 (double mixing)

Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP Teilum
K., Kragelund, BB; Knudsen, J; Poulsen
FM JOURNAL OF MOLECULAR BIOLOGY, 301: (5) 1307-1314 SEP 1 2000
(SFM-400 / quench)

Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue
Garcia, C. Nishimura, C., Cavagnero, S., Dyson, HJ, Wright
PE BIOCHEMISTRY, 39: (37) 11227-11237 SEP 19 2000
(http://pubs.acs.org/isubscribe/journals/bichaw/39/i37/pdf/bi0010266.pdf) note
(QFM-5)

Identifying the Site of Initial Tertiary Structure Disruption during Apomyoglobin Unfolding
Zhaoyang Feng, Jeung-Hoi Ha, and Stewart N. Loh
Biochemistry, 38 , 14433 -14439, 1999.
(SFM-4/QS)

Relationship between the Native-State Hydrogen Exchange and the Folding Pathways of Barnase
Rui-Ai Chu, Jiro Takei, Joseph J. Barchi, Jr., and Yawen Bai
Biochemistry, 38 (43), 14119 -14124, 1999.
(SFM-4/QS)

Rapid GTP binding and hydrolysis by Gq promoted by receptor and GTPase-activating proteins
SUCHETANA MUKHOPADHYAY AND ELLIOTT M. ROSS
Proc. Natl. Acad. Sci. USA – Vol. 96, pp. 9539–9544, August 1999
(http://intl.pnas.org/cgi/content/abstract/96/17/9539) note
(Low-volume, multi-step quenched-flow assay with SFM-4/Q)

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
Joseph E. Coyle, Frieda L. Texter, Alison E. Ashcroft, Dimitris Masselos, Carol V. Robinson & Sheena E. Radford.
Nature structural Biology July 1999 Volume 6 Number 7 pp 683 – 690
(QFM-5 and hydrogen exchange)

Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
VICKIE TSUI, CARLOS GARCIA, SILVIA CAVAGNERO, GARY SIUZDAK, H. JANE DYSON, and PETER E. WRIGHT.
Protein Science (1999), 8: 45-49.
(http://www.prosci.org/cgi-bin/sgmhtm.short.pl?Vol8No01/8189) note
(QFM-5 coupled to mass spectrometry)

R-Lytic Protease Precursor: Characterization of a Structured Folding Intermediate
D. Eric Anderson, Reuben J. Peters, Barry Wilk, and David A. Agard.
Biochemistry 1999, 38, 4728-4735
(CD with SFM-4/S + Jasco and SFM-4/Q)

Folding Kinetics of Villin 14T, a Protein Domain with a Central -Sheet and Two Hydrophobic Cores
Sung E. Choe, Paul T. Matsudaira, John Osterhout, Gerhard Wagner, and Eugene I. Shakhnovich.
Biochemistry 1998, 37 (41), 14508 -14518
(QFM-5 NMR + Mass spectrometry)

Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange
Jeung-Hoi Ha & Stewart N. Loh.
Nature Structural Biology, 1998, Volume 5, pp 730 – 737

Amide protection in an early folding intermediate of cytochrome c
J Michael Sauder, Heinrich Roder.
Folding & Design 19 June 1998, 3:293-301
(http://biomednet.com/library/abstract/JFAD.fd3408) note

Kinetics of Cytochrome c Folding Examined by Hydrogen Exchange and Mass Spectrometry
Houjun Yang and David L. Smith.
(1997) Biochemistry, 36, 14992-14999.

Kinetics of Folding of the IgG Binding Domain of Peptostreptoccocal Protein L
Scalley, M.L., Yi, Q., Gu, H., McCormack, A., Yates III, J.R., and Baker, D.
(1997) Biochemistry, 36, 3373-3382.

Following protein folding in real time using NMR spectroscopy
Balbach, J., Forge, V., van Nuland, N.A.J., Winder, S.L., Hore, P.J. and Dobson, C.M.
(1995) Nature Structural Biology, 2, 865-870.

Folding of a Four-Helix Bundle: Studies of Acyl-Coenzyme A Binding Protein
Kragelund, B.B., Robinson, C.V., Knudsen, J., Dobson, C.M., and Poulsen, F.M.
(1995) Biochemistry, 34, 7217-7224.

Kinetic mechanism of cytochrome c folding : involvement of the heme and its ligands
G.A. Elöve, A.K. Bhuyan and H. Roder.
Biochemistry 1994 33 6925-6935

Kinetic Consequences of the Removal of a Disulfide Bridge on the Folding of Hen Lysozyme
Eyles, S.J., Radford, S.E., Robinson, C.V., and Dobson, C.M.
(1994), 33, 13038-13048.

The refolding of human lysozyme: a comparaison with the structurally homologous hen lysozyme
Hooke, S.D., Radford, S.E. and Dobson, C.M.
(1994) Biochemistry, 33, 5867-5876.

Understanding how proteins fold: the lysozyme story so far
Dobson, C.M., Evans, P.A. and Radford, S.E.
(1994) TIBS, 19, 31-37.

Staphylococcal nuclease folding intermediate characterized by hydrogen excahnge and NMR spectroscopy
Jacobs, M.D. and Fox R.O.
(1994) PNAS 91, 449-453.

The barriers in protein folding
Sosnick, T.R., Mayne, L., Hiller, R. and Englander, S.W.
(1994) Nature Structural Biology 1, 149-155.

Kinetic consequences of the removal of a disulfide bridge on the folding of Hen lysozyme
Eyles, S.J., Radford, S.E., Robinson, C.V. and Dobson, C.M.
(1994) Biochemistry, 33, 13038-13048.

Ca2+ binding to sarcoplasmic reticulum ATPase revisited. II. Equilibrium and kinetic evidence for a two-route mechanism.
Forge V, et al.
J Biol Chem. 1993 May 25;268(15):10961-8.

Rapid kinetic measurements of Second Messenger Formation in olfactory Cilia from Channel Catfish
Restrepo, D., Boekhogg, I., and Breer, H.
(1993) Am. J. Physiol. 264, 906-911.

Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin
Jennings, P.A. and Wright, P.E.
(1993) Science, 262, 892-896.

Investigation of Ribonuclease T1 folding intermediates by Hydrogen-deuterium Amide exchange-two-dimensional NMR spectroscopy.
Mullins, L.S., Pace, C.N., and Raushel, F.M.
(1993) Biochemistry, 32, 6152-6156.

Kinetics of Folding of the Al 1- Sheet Protein Interleukin-l.
Varley, P., Gronenborn, A.M., Christensen, H., Wingfield, P.T., Pain, R.H., and Clore, G.M.
(1993) Science, 260, 1110-1113.

The reaction mechanism of Ca(2+)-ATPase of sarcoplasmic reticulum. Direct measurement of the Mg.ATP dissociation constant gives similar values in the presence or absence of calcium.
Lacapere JJ; Guillain F
Eur J Biochem 1993 Jan 15;211(1-2):117-26

Early hydrogen-bonding events in the folding reaction of ubiquitin
MS Briggs and H. Roder.
PNAS 1992, 89, 2017-2021

The folding of hen lysozyme involves partially structured intermediates and multiple pathways.
Radford, S.E., Dobson, C.M. and Evans, P.A.
(1992) Nature, 358, 302-307.

Kinetics of calcium dissociation from its high-affinity transport sites on sarcoplasmic reticulum ATPase.
Orlowsli, S. and Champeil, P.
(1991) Biochemistry, 30, 352-361.

Reversal of the sarcoplasmic reticulum ATPase cycle by substituting various cations for magnesium. Phosphorylation and ATP synthesis when Ca2+ replaces Mg2+.
Mintz E, et al.
J Biol Chem. 1990 Nov 5;265(31):18762-8.

Rapid kinetics of second messenger formation in olfactory transduction.
Breer, H., Boekhoff I. and Tareilus, E.
(1990) Nature, 345, 65-68.

Stopped flow and rapid quenching measurement of the transient steps induced
by calcium binding to sarcoplasmic reticulum adenosine triphosphatase. Competition with Ca2+-independent phosphorylation.
Guillain F, et al.
J Biol Chem. 1981 Jun 25;256(12):6140-7.

Reaction mechanism of Ca2+ ATPase of sarcoplasmic reticulum. Equilibrium and transient study of phosphorylation with Ca.ATP as substrate.
Lacapere JJ, et al.
J Biol Chem. 1990 May 25;265(15):8583-9.

TOP 

Optical quench-flow

Probing the Reorganization of the Nicotinic Acetylcholine Receptor during Desensitization by Time-Resolved Covalent Labeling Using [3H]AC5, a Photoactivatable Agonist
Alexandre Mourot,1 Jordi Rodrigo,2 Florence Kotzyba-Hibert, Sonia Bertrand, Daniel Bertrand, and Maurice Goeldner
Mol Pharmacol 69:452–461, 2006.
(http://molpharm.aspetjournals.org/cgi/reprint/69/2/452) note 
(SFM-300 + optical quench option)

Structural reorganization of the Acetylcholine binding site of the Torpedo nicotinic receptor as revealed by dynamic photoaffinity labeling
Thomas Grutter, Sonia Bertrand, Florence Kotzyba-Hibert, Daniel Bertrand, Maurice Goeldner
ChemBioChem 2002, 3, 652-658
(SFM-300 + Special optical quench option)

TOP 

Freeze quenched

Structure and Electronic Configurations of the Intermediates of Water Oxidation in Blue Ruthenium Dimer Catalysis
Dooshaye Moonshiram, Jonah Jurss, Javier Concepcion, Taisiya Zakharova, Igor Alperovich, Thomas Meyer, Pushkar, Yulia.
Journal of American Chemical Society, 2012, 134, 4625-4636
(SFM-20 + freeze quench)

Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols
Jeremiah Feducia, Rania Dumarieh, Lauren B. G. Gilvey, Tatyana Smirnova, Stefan Franzen, and Reza A. Ghiladi
Department of Chemistry, North Carolina State UniVersity, Raleigh, North Carolina 27695 Biochemistry 2009, 48, 995–1005
(SFM-400 + freeze quench)

A Calibration Reaction for Rapid Freeze-Quench W-Band EPR
A. Potapov; D. Goldfarb
Applied Magnetic Resonance (2010) 37/845-850
(SFM-300+freeze quench)

An allylic ketyl radical intermediate in clostridial amino-acid fermentation
Jihoe Kim, Daniel J. Darley, Wolfgang Buckel, Antonio J. Pierik
Nature 452, 239-242; 2008
(SFM-20+microvolume freeze quench)

Key feature of the catalytic cycle of TNF-α converting enzyme involves communication between distal protein sites and the enzyme catalytic core
Ariel Solomon, Barak Akabayov, Anatoly Frenkel, Marcos E. Milla, and Irit Sagi
Proc Natl Acad Sci U S A, 2007 March 20; 104(12): 4931–4936.
(SFM-300+ X-ray)

A semiquinone intermediate generated at the Qo site of the cytochrome bc1 complex: Importance for the Q-cycle and superoxide production
Jonathan L. Cape, Michael K. Bowman, and David M. Kramer
Proc Natl Acad Sci U S A. 2007 May 8; 104(19): 7887–7892
(SFM-3 +EPR)

Active site electronic structure and dynamics during metalloenzyme catalysis.
Kleifeld, O., Frenkel, A., Martin, J. M. & Sagi, I. 
Nat. Struct. Biol.
 10, 98-103 (2003).

EPR invertigation of compound 1 in Proteus mirabilis and Bovine liver catalase : formation of porphyrin and tyrosyl radical intermediates
IVANCICH, A., JOUVE, H.M., SARTOR, B. and GAILLARD, J.
Biochemistry, 36, 31, 9356-9364 (1997).

Time-Resolved Solid-State NMR of Enzyme-Substrate Interactions
J.N.S.Evans
contribution for Encyclopedia of NMR, John Wiley & Sons, 4757-4763 (1995).

Time-Resolved Solid-State REDOR NMR Studies of UDP-N-acetylglucosamine Enolpyruvyl Transferase
Y. Li, F. Krekel, C.A.Ramilo, N. Amrhein & J. N. S. Evans.
FEBS Lett. 377, 208-212 (1995).

Time-Resolved Solid-State NMR of EPSP Synthase
R.J.Appleyard, W.A.Shuttleworth & J.N.S.Evans
Biochemistry 33, 6812-6821 (1994).

Time-Resolved Solid-State REDOR NMR Measurements on EPSP Synthase
Y. Li, R.J.Appleyard, W.A.Shuttleworth & J.N.S.Evans.
J.Am. Chem. Soc. 116, 10799-10800 (1994).

Detection of the Covalent Intermediate of UDP-NAG enolpyruvyl transferase by Solution-State and time-Resolved Solid-State NMR
C. Ramilo, R.J.Appleyard, F. Krekel, C. Wanke, N. Amrhein & J. N. S. Evans
Biochemistry 33, 15071-15079 (1994).

Detection of an Enzyme-Intermediate Complex by Time-Resolved Solid-State NMR Spectroscopy
J. N. S. Evans, R. J. Appleyard, and W. A. Shuttleworth.
J.Am.Chem.Soc. 115, 1588-1590 (1993).

Solid State NMR of Glycine in Frozen Solution;
R. J. Appleyard and J. N. S. Evans.
J. Magn. Reson. Series B, 102, 245-252 (1993).

Time-Resolved Solid-State NMR: Small Molecules and Enzymes in Rapidly Frozen Solution
R. J. Appleyard and J. N. S. Evans, Bull.
Magn. Reson.14, 81-85 (1992).

TOP 

Rapid filtration (RFS-4)

Calcium translocation across sarcoplasmic reticulum ATPase randomizes the two transported ions
Canet, D., Forge, V., Guillain, F. and Mintz, E.
(1996) J. Biol. Chem. 271, 20566-20572

Lumenal calcium dissociation from the phosphorylated Ca-ATPase of the sarcoplasmic reticulum is sequential
Forge, V., Mintz, E., Canet, D. and Guillain, F.
(1995) J. Biol. Chem., 270, 18271-18276

Binding of Ca2+ to the (Ca2+-Mg2+)-ATPase of sarcoplasmic reticulum: kinetic studies
Henderson, I.M.J., Starling, A.P., Wictome, M., East, J.M. and Lee, A.G.
(1994) Biochem. J. 297, 625-636.

Mechanism of chloride-dependent release of Ca2+ in the sarcoplasmic reticulum of rabbit skeletal muscle.
Sukhareva, M., Morrissette, J. and Coronado, R.
(1994) Biophysical J. 67, 751-765.

Interdependence of H+ and K+ fluxes during the Ca2+-pumping activity of sarcoplasmic reticulum vesicles
Soler, F., Sanchez-Migallon, P., Gomez-Fernandez, J.C. and Fernandez-Belda, F.
(1994) J. Bioenergetics and Biomembranes 26, 127-136.

Ca²+ binding to sarcoplasmic reticulum ATPase revisited. Equilibrium and kinetic evidence for a two route mechanism.
Forge, V., Mintz, E. and Guillain, F.
(1993) J. Biol. Chem. 268, 10961-10968.

Thapsigargin inhibits contraction and calcium transient in cardiac cells by specific inhibition of the sarcoplasmic reticulum Ca2+ pump
Kirby, M.S., Sagara, Y., Gaa, S., Inesi, G., Lederer, W.J. and Rogers, T.B.
J. Biol. Chem. (1992) 267, 12545-12551.

Characterization of the inhibition of intracellular Ca2+ transport ATPases by Thapsigargin
Sagara, Y., Frenandez-Belda, F., deMeis L., and Inesi, G.
J. Biol. Chem. (1992) 267, 12606-12613

Functional characterisation of lanthanide binding sites in the sarcoplasmic reticulum Ca2+-ATPase – Do lanthanide ions bind to the calcium transport site.
Ogurusus, T., Wakabayashi, S. and Shigekawa, M.
(1991) Biochemistry, 30, 9966-9973.

Does fluorescence of 4-nitrobenzo-2-oxa-1,3-diazole incorporated into sarcoplasmic reticulum ATPase Monitor putative El-E2 conformational transition.
Wakabayashi, S., Imagawa, T. and Shigekawa, M. (1990)
J. Biochem. 107, 563-571.

Mechanism for activation of the 4-Nitrobenzo-2-oxa-1,3-diazole-labeled sarcoplasmic reticulum ATPase by Calcium and its modulation by nucleotides
Wakabayashi, S. and Shigekawa, M. (1990)
Biochemistry, 29, 7309-7318

Effect of halothane on calcium release from sarcoplasmic reticulum of rabbit psoas and semitendinosus skinned muscle fibers.
Carrier, L. k Villaz, M.
(1990) Biochemical Pharmacology,, 39, 145-149.

Calcium and Lanthanide Binding in the sarcoplasmic reticulum ATPase
Squier, C.T., Bigelow, D.J., Fernandez-Belda, J., deMeis, L. and Inesi, G.
(1990) J. Biol. Chem. 265, 13713-13720.

Microassay for malignat hyperthermia susceptibility: hypersensitive ligand-gating of the Ca channel in muscle sarcoplasmic reticulum causes increased amounts and rates of Ca-release
O’Brien
(1990) Molecular and Cellular Biochemistry 93, 53-59

Participation of H+ in the Ca2+-induced conformational transition of 4-nitro-2,1,3-benzoxadiazole-labeled sarcoplasmic reticulum ATPase.
Wakabayashi, S., Ogurusu, T. and Shigekawa, M.
(1990), Biochemistry, 29, 10613-10620.

Activation and inhibition of the calcium-release channel of isolated skeletal muscle heavy sarcoplasmic reticulum.
Wyskovsky, W., Hoheneger, M., Plank, B., Hellmann, G. Klein, S. and Suko, J. (1990)
Eur. J. Biochem. 194, 549-559.

Rapid kinetics of the calcium-release channels of Skeletal Muscle Sarcoplasmic reticulum: the effect of inhibitors.
Calviello, 6. and Chiesi, M.
(1989), Biochemistry, 28, 1301-1306.

Characterization of the tetraphenylboron-induced Calcium release from skeletal muscle sarcoplasmic reticulum.
Soler, F., Fernandez-Belda, F. and Gomez-Fernandez, J.C.
(1989), Eur. J. Biochem. 181, 513-518.

Rapid Ag’-induced release of Ca” from sarcoplasmic reticulum vesicles of skeletal muscle: a rapid filtration study
Moutin, M.J., Abramson, J.J., Salama, G. and Dupont, Y.
(1989), BBA, 984, 289-292.

Quinacrine inhibits the calcium-induced calcium release in heavy sarcoplasmic reticulum vesicles
Fernandez-Belda, F., Soler, F. and Gomez-Fernandez, C.
(1989) BBA

Postulated role of calsequestrine in the regulation of calcium release from sarcoplasmic reticulum from skeletal muscles.
Ikemoto, N., Ronjat, M., Meszaros, L.G. and Koshita, M.
(1989) Biochemistry, 28, 6764-6771.

Polylysine induced rapid calcium release from sarcoplasmic reticulum vesicles by mediation of its binding to the foot protein.
Cifuentes, M.E. and Ronjat, M.
(1989) Arch. Biochem. Biophys. 272, 554-561.

Non-identical behavior of the Ca-ATPase in the terminal cisternae and the longitudinal tubules fractions of sarcoplasmic reticulum
Meszaros, L.G. and Ikemoto, N.
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