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Updated: Sep 28, 2025

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Thermodynamics of globular protein native structure
Nikolay N Khechinashvili1, Maxim S Kondratyev1, Robert V Polozov2
1Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Russia.
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.
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