Aug 1, 1995

Structural energetics of barstar studied by differential scanning microcalorimetry

Protein Science : a Publication of the Protein Society
P L WintrodeP L Privalov

Abstract

The energetics of barstar denaturation have been studied by CD and scanning microcalorimetry in an extended range of pH and salt concentration. It was shown that, upon increasing temperature, barstar undergoes a transition to the denatured state that is well approximated by a two-state transition in solutions of high ionic strength. This transition is accompanied by significant heat absorption and an increase in heat capacity. The denaturational heat capacity increment at approximately 75 degrees C was found to be 5.6 +/- 0.3 kJ K-1 mol-1. In all cases, the value of the measured enthalpy of denaturation was notably lower than those observed for other small globular proteins. In order to explain this observation, the relative contributions of hydration and the disruption of internal interactions to the total enthalpy and entropy of unfolding were calculated. The enthalpy and entropy of hydration were found to be in good agreement with those calculated for other proteins, but the enthalpy and entropy of breaking internal interactions were found to be among the lowest for all globular proteins that have been studied. Additionally, the partial specific heat capacity of barstar in the native state was found to be 0.37 +/- 0.03 cal K...Continue Reading

Mentioned in this Paper

Thermodynamics
Bacterial Proteins
Macromolecular Alteration
Bacillus amyloliquefaciens ribonuclease
Denaturation
Calorimetry, Differential Scanning
Microcalorimetry
Circular Dichroism, Vibrational
Protein Folding, Globular
Protein Denaturation

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