Abstract
General operational principles of a scanning microcalorimeter, methods and approaches to obtaining thermodynamic and kinetic information on the studied transition, and the existence of correlations between the structural features of a macromolecule and the measured thermodynamic parameters of denaturation transitions are considered. The results of studying the domain organization for a number of proteins and transfer poly(ribonucleic acids), the kinetics of heat denaturation, and the nature of the transitional (activated) state of macromolecules are surveyed. The potential of high-pressure scanning microcalorimetry for measuring volume changes during conformational transitions of proteins and lipids is discussed.
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Original Russian Text © S.A. Potekhin, 2012, published in Vysokomolekulyarnye Soedineniya, Ser. C, 2012, Vol. 54, No. 7, pp. 1077–1085.
This work was supported by the Russian Foundation for Basic Research, project no. 11-04-00864-a.
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Potekhin, S.A. The potential of scanning microcalorimetry for studying thermotropic conformational transitions in biomacromolecules1. Polym. Sci. Ser. C 54, 108–115 (2012). https://doi.org/10.1134/S1811238212070053
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DOI: https://doi.org/10.1134/S1811238212070053