Naturally evolving proteins gradually accumulate mutations while continuing to fold to stable structures. This process of neutral evolution is an important mode of genetic change and forms the basis for the molecular clock. We present a mathematical theory that predicts the number of accumulated mutations, the index of dispersion, and the distribution of stabilities in an evolving protein popul...

A new approach to study the thermodynamics of salt-protein interaction is described using a protein-ligand binding system. The effects of salts on the thermodynamics of association or dissociation of the ligand are related to the effect on the hydrophobic side chains on the interior of the protein by these salts. The calculated free energies of transfer of a methylene group from an interior of ...

The capabilities of contemporary differential scanning and isothermal titration microcalorimetry for studying the thermodynamics of protein unfolding/refolding and their association with partners, particularly target DNA duplexes, are considered. It is shown that the predenaturational changes of proteins must not be ignored in studying the thermodynamics of formation of their native structure a...