Synergism between x-ray crystallography and NMR residual dipolar couplings in characterizing protein dynamics.

ABSTRACT: The important role of structural dynamics in protein function is widely recognized. Thermal or B-factors and their anisotropy, seen in x-ray analysis of protein structures, report on the presence of atomic coordinate heterogeneity that can be attributed to motion. However, their quantitative evaluation in terms of protein dynamics by x-ray ensemble refinement remains challenging. NMR spectroscopy provides quantitative information on the amplitudes and time scales of motional processes. Unfortunately, with a few exceptions, the NMR data do not provide direct insights into the atomic details of dynamic trajectories. Residual dipolar couplings, measured by solution NMR, are very precise parameters reporting on the time-averaged bond-vector orientations and may offer the opportunity to derive

SUBMITTER: Shen Y 

PROVIDER: S-EPMC10338066 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature