Jump to main content
Jump to site search

Issue 1, 2017
Previous Article Next Article

A driving force for polypeptide and protein collapse

Author affiliations

Abstract

Experimental measurements and computational results have shown that polypeptide chains, made up of 15–25 glycine residues, collapse to compact structures in water at room temperature. This contrasts with the classic idea that the burial of nonpolar side chains, i.e., the hydrophobic effect, is the driving force of collapse and folding of polypeptides and proteins. It is thus necessary to find a different driving force for polyglycine collapse. The present study aims at showing that the hydrophobic effect has to be re-defined in terms of decrease in solvent-excluded volume associated with chain collapse so that it is characterized by a gain in translational entropy of water molecules. This indicates that the presence of nonpolar side chains is not so important for polypeptide and protein collapse, even though it may be fundamental for the attainment of a unique folded structure.

Graphical abstract: A driving force for polypeptide and protein collapse

Back to tab navigation

Supplementary files

Publication details

The article was received on 28 Oct 2016, accepted on 02 Dec 2016 and first published on 02 Dec 2016


Article type: Paper
DOI: 10.1039/C6CP07397B
Citation: Phys. Chem. Chem. Phys., 2017,19, 751-756

  •   Request permissions

    A driving force for polypeptide and protein collapse

    A. Merlino, N. Pontillo and G. Graziano, Phys. Chem. Chem. Phys., 2017, 19, 751
    DOI: 10.1039/C6CP07397B

Search articles by author

Spotlight

Advertisements