Thermo- and mesostabilizing protein interactions identified by temperature-dependent statistical potentials.

ABSTRACT: The goal of controlling protein thermostability is tackled here through establishing, by in silico analyses, the relative weight of residue-residue interactions in proteins as a function of temperature. We have designed for that purpose a (melting-) temperature-dependent, statistical distance potential, where the interresidue distances are computed between the side-chain geometric centers or their functional centers. Their separate derivation from proteins of either high or low thermal resistance reveals the interactions that contribute most to stability in different temperature ranges. Thermostabilizing interactions include salt bridges and cation-pi interactions (especially those involving arginine), aromatic interactions, and H-bonds between negatively charged and some aromatic residues

SUBMITTER: Folch B 

PROVIDER: S-EPMC2820637 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature