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Thermodynamics of bpti folding

โœ Scribed by George I. Makhatadze; Key-Sun Kim; Clare Woodward; Peter L. Privalov

Book ID
105356178
Publisher
Cold Spring Harbor Laboratory Press
Year
1993
Tongue
English
Weight
790 KB
Volume
2
Category
Article
ISSN
0961-8368

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โœฆ Synopsis

Abstract

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 5โ€“130 ยฐC. 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 ยฐC 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.

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