通过核磁共振探测分子运动。

Probing molecular motion by NMR.

作者信息

Palmer A G

机构信息

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

出版信息

Curr Opin Struct Biol. 1997 Oct;7(5):732-7. doi: 10.1016/s0959-440x(97)80085-1.

DOI:10.1016/s0959-440x(97)80085-1

PMID:9345634

Abstract

Recently developed solution NMR methods for measuring 2H, 13C, and 15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins.

摘要

最近开发的用于测量2H、13C和15N自旋弛豫的溶液核磁共振方法，结合生物合成同位素富集，能够在皮秒/纳秒和微秒/毫秒时间尺度上表征蛋白质主链和侧链的动力学性质。对弛豫数据的理论解释有助于深入了解蛋白质的生物物理和功能特性。