THERMODYNAMICS OF BPTI FOLDING

被引：93

作者：

MAKHATADZE, GI

KIM, KS

WOODWARD, C

PRIVALOV, PL

机构：

[1] JOHNS HOPKINS UNIV,DEPT BIOL,3400 N CHARLES ST,BALTIMORE,MD 21218

[2] UNIV MINNESOTA,DEPT BIOCHEM,ST PAUL,MN 55108

[3] JOHNS HOPKINS UNIV,CTR BIOCALORIMETR,BALTIMORE,MD 21218

来源：

PROTEIN SCIENCE | 1993年 / 2卷 / 12期

关键词：

BPTI; HEAT CAPACITY; SCANNING MICROCALORIMETRY; STABILITY;

D O I：

10.1002/pro.5560021204

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：

A calorimetric study of the basic pancreatic trypsin inhibitor (BPTI) has been performed using the new generation of the adiabatic scanning microcalorimeters, operating in an extended temperature range of 5-130-degrees-C. Precise measurements of the heat capacities of the native and unfolded states of BPTI show that the heat capacity change upon unfolding strongly depends on temperature; its value is maximal at about 50-degrees-C and diminishes as the temperature is increased. The temperature dependencies of the enthalpy and entropy changes upon BPTI unfolding were found to be similar to those normally observed for other small globular proteins. The stability of BPTI has been correlated with its structure.

引用

页码：2028 / 2036

页数：9

共 48 条

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