Premium
Multi‐Timescale Conformational Dynamics of the SH3 Domain of CD2‐Associated Protein using NMR Spectroscopy and Accelerated Molecular Dynamics
Author(s) -
Salmon Loïc,
Pierce Levi,
Grimm Alexander,
Ortega Roldan JoseLuis,
Mollica Luca,
Jensen Malene Ringkjøbing,
van Nuland Nico,
Markwick Phineus R. L.,
McCammon J. Andrew,
Blackledge Martin
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201202026
Subject(s) - dynamics (music) , molecular dynamics , sh3 domain , protein dynamics , residual dipolar coupling , nuclear magnetic resonance spectroscopy , picosecond , chemical physics , millisecond , chemistry , biophysics , spectroscopy , nuclear magnetic resonance , biological system , crystallography , physics , computational chemistry , biology , optics , biochemistry , laser , kinase , astronomy , quantum mechanics , acoustics , proto oncogene tyrosine protein kinase src
An extensive set of experimental NMR residual dipolar couplings (RDCs) has been used to determine the conformational behavior of the SH3 domain of CD2‐associated protein. Analytical descriptions of the local dynamics were compared to restraint‐free accelerated molecular dynamics simulation, providing a convergent and comprehensive description of conformational fluctuations on picosecond to millisecond timescales.