PROTEIN DYNAMICS

被引：23

作者：

JARDETZKY, O ^{[1
]}

LEFEVRE, JF ^{[1
]}

机构：

[1] INST BIOL MOLEC & CELLULAIRE, F-67084 STRASBOURG, FRANCE

来源：

FEBS LETTERS | 1994年 / 338卷 / 03期

关键词：

PROTEIN; DYNAMICS; FOLDING; NMR; RELAXATION;

D O I：

10.1016/0014-5793(94)80277-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Modern NMR has revitalized the study of protein dynamics. Multidimensional spectra and the heteronuclear spectroscopy allow a substantial gain in resolution. Dynamics can be analyzed at individual sites and data on segmental and sequence-dependent flexibility are accumulating. This review summarizes the wide variety of NMR approaches for observing internal motions, including the folding processes, and the attempts to correlate dynamics to the biological activity of proteins. The implications of mobility on structure determination by NMR is also discussed.

引用

页码：246 / 250

页数：5

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