Suivre
Guillaume Bouvignies
Guillaume Bouvignies
Department of Chemistry, École Normale Supérieure, Paris
Adresse e-mail validée de ens.psl.eu - Page d'accueil
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Studying “invisible” excited protein states in slow exchange with a major state conformation
P Vallurupalli, G Bouvignies, LE Kay
Journal of the American Chemical Society 134 (19), 8148-8161, 2012
4772012
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
G Bouvignies, P Vallurupalli, DF Hansen, BE Correia, O Lange, A Bah, ...
Nature 477 (7362), 111-114, 2011
3072011
Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings
G Bouvignies, P Bernadó, S Meier, K Cho, S Grzesiek, R Brüschweiler, ...
Proceedings of the National Academy of Sciences of the United States of …, 2005
2852005
Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy
PRL Markwick, G Bouvignies, M Blackledge
Journal of the American Chemical Society 129 (15), 4724-4730, 2007
1832007
Toward a unified representation of protein structural dynamics in solution
PRL Markwick, G Bouvignies, L Salmon, JA McCammon, M Nilges, ...
Journal of the American Chemical Society 131 (46), 16968-16975, 2009
1222009
Protein Conformational Flexibility from Structure‐Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin
L Salmon, G Bouvignies, P Markwick, N Lakomek, S Showalter, DW Li, ...
Angewandte Chemie International Edition 48 (23), 4154-4157, 2009
1142009
Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways
A Sekhar, JAO Rumfeldt, HR Broom, CM Doyle, G Bouvignies, ...
elife 4, e07296, 2015
1132015
Mapping the conformation of a client protein through the Hsp70 functional cycle
A Sekhar, R Rosenzweig, G Bouvignies, LE Kay
Proceedings of the National Academy of Sciences 112 (33), 10395-10400, 2015
1022015
Hsp70 biases the folding pathways of client proteins
A Sekhar, R Rosenzweig, G Bouvignies, LE Kay
Proceedings of the National Academy of Sciences 113 (20), E2794-E2801, 2016
982016
A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
G Bouvignies, LE Kay
Journal of biomolecular NMR 53, 303-310, 2012
932012
Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings
G Bouvignies, P Markwick, R Brüschweiler, M Blackledge
Journal of the American Chemical Society 128 (47), 15100-15101, 2006
862006
Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions
A Sekhar, A Velyvis, G Zoltsman, R Rosenzweig, G Bouvignies, LE Kay
Elife 7, e32764, 2018
802018
Structure and dynamics of the MKK7–JNK signaling complex
J Kragelj, A Palencia, MH Nanao, D Maurin, G Bouvignies, M Blackledge, ...
Proceedings of the National Academy of Sciences 112 (11), 3409-3414, 2015
782015
Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer
G Bouvignies, LE Kay
The Journal of Physical Chemistry B 116 (49), 14311-14317, 2012
752012
Increasing the Exchange Time-Scale That Can Be Probed by CPMG Relaxation Dispersion NMR
P Vallurupalli, G Bouvignies, LE Kay
The Journal of Physical Chemistry B, 2011
742011
13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics
AJ Baldwin, TL Religa, DF Hansen, G Bouvignies, LE Kay
Journal of the American Chemical Society, 2010
712010
Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy
E Delaforge, J Kragelj, L Tengo, A Palencia, S Milles, G Bouvignies, ...
Journal of the American Chemical Society 140 (3), 1148-1158, 2018
662018
Visualizing side chains of invisible protein conformers by solution NMR
G Bouvignies, P Vallurupalli, LE Kay
Journal of molecular biology 426 (3), 763-774, 2014
662014
Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings
G Bouvignies, PRL Markwick, M Blackledge
Chemphyschem 8 (13), 1901-1909, 2007
612007
Nuclear Magnetic Resonance Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Time Scales
L Salmon, G Bouvignies, P Markwick, M Blackledge
Biochemistry 50 (14), 2735-2747, 2011
572011
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