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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.
Salmon et al. (Tue,) studied this question.