PROTEIN DYNAMICS STUDIED BY HETERONUCLEAR MULTI-DIMENSIONAL NMR

Abstract

Abstract:

One of the fundamental problems in understanding life science at the molecular level is the relationship among structure, dynamics, and function of proteins. NMR has a unique capacity to investigate dynamics properties of proteins over a range of different time scales with atomic resolution. This review focuses on the experimental and theoretical methods used in heteronuclear spin relaxation measurement for studying protein dynamics, and the parameters describing the protein internal motion as well as the Model-Free method. Finally, some application examples are given in which ¹⁵N relaxation measurements were performed to study the backbone dynamics of protein and protein-ligand complex.

Key words: protein, relaxation, dynamics, mobility, heteronuclear NMR

CLC Number:

O482.53

LIAO Xin-Li, Lin-Dong-Hai. PROTEIN DYNAMICS STUDIED BY HETERONUCLEAR MULTI-DIMENSIONAL NMR[J]. Chinese Journal of Magnetic Resonance, 2004, 21(4): 385-396.

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