Thermodynamics of BPTI folding.


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 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. Study holds ProTherm entries: 2786, 2787, 2788, 2789, 2790, 2791 Extra Details: BPTI; heat capacity; scanning microcalorimetry; stability

Submission Details

ID: tmbxN9nC

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:19 p.m.

Version: 1

Publication Details
Makhatadze GI;Kim KS;Woodward C;Privalov PL,Protein Sci. (1993) Thermodynamics of BPTI folding. PMID:7507751
Additional Information

Sequence Assay Result Units