Translational-entropy gain of solvent upon protein folding.

ABSTRACT: We show that even in the complete absence of potential energies among the atoms in a protein-aqueous solution system, there is a physical factor that favors the folded state of the protein. It is a gain in the translational entropy (TE) of water originating from the translational movement of water molecules. An elaborate statistical-mechanical theory is employed to analyze the TE of water in which a protein or peptide with a prescribed conformation is immersed. It is shown that if the number of residues is sufficiently large, the TE gain is powerful enough to compete with the conformational-entropy loss upon folding. For protein G we have tested over 100 compact conformations generated by a computer simulation with the all-atom potentials as well as the native structure. A significant find

SUBMITTER: Harano Y 

PROVIDER: S-EPMC1366771 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature