Cold denaturation of ubiquitin

被引：65

作者：

Ibarra-Molero, B

Makhatadze, GI

Sanchez-Ruiz, JM ^{[1
]}

机构：

[1] Univ Granada, Fac Ciencias, Dept Quim Fis, E-18071 Granada, Spain

[2] Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1429卷 / 02期

关键词：

ubiquitin; guanidinium hydrochloride; cold denaturation; differential scanning calorimetry; protein stability; chemical denaturation;

D O I：

10.1016/S0167-4838(98)00252-0

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：

Temperature induced unfolding of bovine ubiquitin in solutions with different concentrations of guanidinium hydrochloride (GdmCl) has been measured using differential scanning calorimetry. It has been shown that at high concentrations of GdmCl the ubiquitin molecule can undergo both heat and cold induced denaturation. Analysis of the enthalpy of unfolding of ubiquitin in the presence of GdmCl shows a good agreement with the thermodynamic denaturant binding model. The unfolding Gibbs energy is found to change linearly with guanidine concentration up to zero denaturant concentration. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：384 / 390

页数：7

共 17 条

[1] AN OSMOLYTE EFFECT ON THE HEAT-CAPACITY CHANGE FOR PROTEIN-FOLDING [J].