Protein Dynamics Studied by NMR Spin Relaxation

Abstract

Abstract:

A static three-dimensional structure alone does not fully interpret the physiological functions of a protein in many cases. Dynamics studies can disclose internal motions of a protein on different time scales, providing a better link between dynamic structures and biological functions. In this review, the theoretical and experimental methods for protein dynamics studied by NMR spin relaxation are summarized. The reduced spectral density mapping and the Modelfree formulism are employed to describe fast motions on the ps~ns time scale. Slow motions on the μs~ms time scale, associated with conformational and chemical exchanges, are often analyzed by CPMG and R_1ρ relaxation dispersion curves. NMR-based dynamics studies promote protein structures from the three-dimensional date to the fourdimensional era.

Key words: NMR, protein, dynamics, spin relaxation

CLC Number:

O482.53
Q51

WEN Yi, LIN Dong-Hai. Protein Dynamics Studied by NMR Spin Relaxation[J]. Chinese Journal of Magnetic Resonance, 2012, 29(2): 288-306.

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