Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group

被引：320

作者：

Lim, Woon Ki ^{[2
,3
]}

Rosgen, Jorg ^{[1
]}

Englander, S. Walter ^{[2
]}

机构：

[1] Univ Texas Med Branch, Dept Biochem & Mol Biol, Galveston, TX 77555 USA

[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[3] Pusan Natl Univ, Coll Nat Sci, Dept Mol Biol, Pusan 609735, South Korea

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2009年 / 106卷 / 08期

基金：

美国国家卫生研究院;

关键词：

denaturation; hydrogen exchange; osmolyte; solvation; MOLECULAR-DYNAMICS; PREFERENTIAL SOLVATION; AMINO-ACIDS; WATER; DENATURATION; HYDROCHLORIDE; ENERGETICS; STABILITY; CHLORIDE; PROTON;

D O I：

10.1073/pnas.0812588106

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：

The mechanism by which urea and guanidinium destabilize protein structure is controversial. We tested the possibility that these denaturants form hydrogen bonds with peptide groups by measuring their ability to block acid- and base-catalyzed peptide hydrogen exchange. The peptide hydrogen bonding found appears sufficient to explain the thermodynamic denaturing effect of urea. Results for guanidinium, however, are contrary to the expectation that it might H-bond. Evidently, urea and guanidinium, although structurally similar, denature proteins by different mechanisms.

引用

页码：2595 / 2600

页数：6

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