Glassy Dynamics of Side-Chain Ordering in a Simple Model of Protein Folding

Edo Kussell, Eugene I. Shakhnovich

Research output: Contribution to journalArticle

Abstract

We introduce a modified version of protein lattice models in which monomers have several spin states, representing side-chain rotamers. Completion of folding corresponds to reaching the native backbone configuration with complete ordering of side chains. We find that as temperature is lowered, side-chain ordering becomes much slower than backbone folding. The presence of side chains leads to nonexponential kinetics and a broad distribution of relaxation times.

Original languageEnglish (US)
JournalPhysical Review Letters
Volume89
Issue number16
DOIs
StatePublished - Jan 1 2002

    Fingerprint

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this