Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR.

ABSTRACT: Detailed descriptions of atomic coordinates and motions are required for an understanding of protein dynamics and their relation to molecular recognition, catalytic function, and allostery. Historically, NMR relaxation measurements have played a dominant role in the determination of the amplitudes and timescales (picosecond-nanosecond) of bond vector fluctuations, whereas high-resolution X-ray diffraction experiments can reveal the presence of and provide atomic coordinates for multiple, weakly populated substates in the protein conformational ensemble. Here we report a hybrid NMR and X-ray crystallography analysis that provides a more complete dynamic picture and a more quantitative description of the timescale and amplitude of fluctuations in atomic coordinates than is obtainable from th

SUBMITTER: Fenwick RB 

PROVIDER: S-EPMC3910589 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature