UREA-GENERATED FREE ROTATING WATER-MOLECULES ARE ACTIVE IN THE PROTEIN UNFOLDING PROCESS

被引：9

作者：

KHURGIN, Y

MAKSAREVA, E

机构：

[1] N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, 117913

来源：

FEBS LETTERS | 1993年 / 315卷 / 02期

关键词：

PROTEIN UNFOLDING; UREA; WATER SYSTEM; UV-DIFFERENCE AND MILLIMETER SPECTROSCOPY;

D O I：

10.1016/0014-5793(93)81152-P

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 critical urea concentration (C3*) which destabilizes the structure of bovine serum albumin and chymotrypsinogen was determined by UV difference spectroscopy. The increase of the relative content of mobile rotating water molecules in aqueous urea was formerly shown by millimeter spectroscopy [1]. The rise of rotator content at a urea concentration C3 greater-than-or-equal-to C3* when the bulk water is practically exhausted is suggested as a main driving force of protein unfolding.

引用

页码：149 / 152

页数：4

共 15 条

[1] PROTEIN STABILIZATION AND DESTABILIZATION BY GUANIDINIUM SALTS [J].