NMR DETERMINATION OF RESIDUAL STRUCTURE IN A UREA-DENATURED PROTEIN, THE 434-REPRESSOR

被引：481

作者：

NERI, D ^{[1
]}

BILLETER, M ^{[1
]}

WIDER, G ^{[1
]}

WUTHRICH, K ^{[1
]}

机构：

[1] SWISS FED INST TECHNOL,INST MOLEK BIOL & BIOPHYS,CH-8092 ZURICH,SWITZERLAND

来源：

SCIENCE | 1992年 / 257卷 / 5076期

关键词：

D O I：

10.1126/science.1523410

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain of the 434-repressor and distance geometry calculations showed that the polypeptide segment 54 to 59 forms a hydrophobic cluster containing the side chains of Val54, Val56, Trp58, and Leu59. This residual structure in the urea-unfolded protein is related to the corresponding region of the native, folded protein by simple rearrangements of the residues 58 to 60. Based on these observations a model for the early phase of refolding of the 434-repressor(1-63) is proposed.

引用

页码：1559 / 1563

页数：5

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