Structure of the pressure-assisted cold denatured state of ubiquitin

被引：41

作者：

Nash, DP

Jonas, J

机构：

[1] UNIV ILLINOIS,SCH CHEM SCI,DEPT CHEM,URBANA,IL 61801

[2] UNIV ILLINOIS,BECKMAN INST ADV SCI & TECHNOL,URBANA,IL 61801

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1997年 / 238卷 / 02期

关键词：

D O I：

10.1006/bbrc.1997.7308

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：

The pressure-assisted cold denatured state of ubiquitin in aqueous solution was investigated by high resolution NMR. Hydrogen exchange kinetics were measured for backbone amide protons in the cold denatured protein to determine its structure, In contrast to cold denatured ribonuclease A and lysozyme, cold denatured ubiquitin shows little persistent secondary structure. The behavior of ubiquitin supports the idea of a relationship between the residual structure of pressure-assisted cold-denatured states and the structure of early folding intermediates provided they exist. (C) 1997 Academic Press.

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收藏

页码：289 / 291

页数：3

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