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THERMODYNAMICS OF UBIQUITIN UNFOLDING

被引：167
作者：
WINTRODE, PL
MAKHATADZE, GI
PRIVALOV, PL
机构：
[1] JOHNS HOPKINS UNIV, DEPT BIOL, BALTIMORE, MD 21218 USA
[2] JOHNS HOPKINS UNIV, CTR BIOCALORIMETR, BALTIMORE, MD 21218 USA
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 1994年 / 18卷 / 03期
关键词：
MICROCALORIMETRY; HEAT CAPACITY; ENTHALPY; HYDROGEN BONDING;
D O I：
10.1002/prot.340180305
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 energetics of ubiquitin unfolding have been studied using differential scanning microcalorimetry. For the first time it has been shown directly that the enthalpy of protein unfolding is a nonlinear function of temperature. Thermodynamic parameters of ubiquitin unfolding were correlated with the structure of the protein. The enthalpy of hydrogen bonding in ubiquitin was calculated and compared to that obtained for other proteins. It appears that the energy of hydrogen bonding correlates with the average length of the hydrogen bond in a given protein structure. (C) 1994 Wiley-Liss, Inc.
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页码：246 / 253
页数：8
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