Multi‐Timescale Conformational Dynamics of the SH3 Domain of CD2‐Associated Protein using NMR Spectroscopy and Accelerated Molecular Dynamics

Abstract

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.