NMR ASSIGNMENTS AS A BASIS FOR STRUCTURAL CHARACTERIZATION OF DENATURED STATES OF GLOBULAR-PROTEINS

被引：86

作者：

WUTHRICH, K

机构：

[1] Institut für Molekularbiologie und Biophysik, Eidgenössiche Technische Hochschule-Hönggerberg

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1994年 / 4卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(94)90065-5

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：

NMR has unique potential for detailed structural characterization of denatured states of proteins, provided that workable spectral resolution and sequence-specific assignments can be obtained in spite of the lack of conformation-dependent dispersion of the H-1 chemical shifts. Structures can be determined in the presence of dynamic conformational polymorphism. This has recently been achieved for urea-unfolded bacteriophage 434 repressor, and NMR assignments were determined for urea-unfolded FK 506-binding protein.

引用

页码：93 / 99

页数：7

共 28 条

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