MULTIDIMENSIONAL NUCLEAR-MAGNETIC-RESONANCE METHODS FOR PROTEIN STUDIES

被引：186

作者：

BAX, A

机构：

[1] National Institutes of Health, Bethesda

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1994年 / 4卷 / 05期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0959-440X(94)90173-2

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：

Nuclear magnetic resonance (NMR) technology has advanced significantly over the past few years. After the initial development of three- and four-dimensional NMR spectroscopy, several important improvements on these experiments have been made; these offer significantly higher sensitivity and improved resolution, resulting in additional structural constraints. Other methodological improvements now make it possible to obtain complete resonance assignments, even in partially denatured proteins, opening new windows for studying the protein folding problem.

引用

页码：738 / 744

页数：7

共 49 条

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[8] LOCALIZATION OF BOUND WATER IN THE SOLUTION STRUCTURE OF A COMPLEX OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 WITH DNA
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[9] A CONSTANT-TIME 3-DIMENSIONAL TRIPLE-RESONANCE PULSE SCHEME TO CORRELATE INTRARESIDUE H-1(N), N-15, AND C-13(') CHEMICAL-SHIFTS IN N-15-C-13-LABELED PROTEINS
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