Apr 1, 1994

Thermodynamics of barnase unfolding

Protein Science : a Publication of the Protein Society
Y V GrikoR W Hartley


The thermodynamics of barnase denaturation has been studied calorimetrically over a broad range of temperature and pH. It is shown that in acidic solutions the heat denaturation of barnase is well approximated by a 2-state transition. The heat denaturation of barnase proceeds with a significant increase of heat capacity, which determines the temperature dependencies of the enthalpy and entropy of its denaturation. The partial specific heat capacity of denatured barnase is very close to that expected for the completely unfolded protein. The specific denaturation enthalpy value extrapolated to 130 degrees C is also close to the value expected for the full unfolding. Therefore, the calorimetrically determined thermodynamic characteristics of barnase denaturation can be considered as characteristics of its complete unfolding and can be correlated with structural features--the number of hydrogen bonds, extent of van der Waals contacts, and the surface areas of polar and nonpolar groups. Using this information and thermodynamic information on transfer of protein groups into water, the contribution of various factors to the stabilization of the native structure of barnase has been estimated. The main contributors to the stabilization ...Continue Reading

  • References29
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Mentioned in this Paper

Alkalescens-Dispar Group
Bacillus amyloliquefaciens ribonuclease
Alkaline Ribonuclease
Sternal Cleft
Hydrogen Bonding
Hydrophobic Interactions
Protein Folding, Globular

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