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

被引:482
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
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
收藏
页码:1559 / 1563
页数:5
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