Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins.

ABSTRACT: Growing evidence suggests that the conformational distributions of amino acid residues in unfolded peptides and proteins depend on the nature of the nearest neighbors. To explore whether the underlying interactions would lead to a breakdown of the isolated pair hypothesis of the classical random coil model, we further analyzed the conformational propensities that were recently obtained for the two guest residues (x,y) of GxyG tetrapeptides. We constructed a statistical thermodynamics model that allows for cooperative as well as for anticooperative interactions between adjacent residues adopting either a polyproline II or a β-strand conformation. Our analysis reveals that the nearest-neighbor interactions between most of the central residues in the investigated GxyG peptides are anticoopera

SUBMITTER: Schweitzer-Stenner R 

PROVIDER: S-EPMC5883598 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature