Thermodynamics of globular protein native structure

Abstract

The temperature dependence of the partial heat capacity of the native protein structure in an aqueous solution has been analyzed. It is shown that the strictly linear temperature dependence is due to the contributions of the vibrational and conformational components, which indicates volume consistensy and the absence of conformational transitions up to the main two-state transition. The two-level structural and functional organization of the protein three-dimensional structure are considered in relation to the energy and conformational entropy properties in accordance with the principles of the organization of the protein macromolecule.

Communicated by Ramaswamy H. Sarma

Keywords:

• Heat capacity
• enthalpy
• entropy
• absolute free energy

Disclosure statement

No potential conflict of interest was reported by the authors.