Masahiro Kinoshita

TL;DR: In this article, the sum of the intramolecular energy and the hydration free energy is defined as the key function for protein folding under the isochoric condition, and the change in this function is governed by the change of hydration entropy, where the protein is designed to fold into the structure that maximizes the entropy of water under the requirement that sufficiently many intramolescular hydrogen bonds be formed to compensate the dehydration penalty.

TL;DR: It is argued for all the four cytochromes c that due to covalent heme linkages, the number of accessible conformations of the denatured state is decreased by the steric hindrance of heme, and the conformational-entropy loss upon folding becomes smaller, leading to an enhancement of the thermal stability.

TL;DR: In this paper, the first principles for peptide and protein conformations in aqueous solution were developed and the results of the first attempt to combine the multicanonical algorithm for extensive sampling of the phase space and the reference interaction site model (RISM) theory for incorporating solvent effects.

TL;DR: The theoretical results are in qualitatively good accord with the experimental observations for the rotational mobility of water molecules near nonpolar side chains of amino acids and F-actin with the domains which are rich in negative charges.