Glassy dynamics of side-chain ordering in a simple model of protein folding

Edo Kussell, Eugene I. Shakhnovich

Research output: Contribution to journalArticle

Abstract

Using simple lattice simulations, it was demonstrated that full side-chain relaxation during protein folding can be a much slower process than backbone folding. While backfolding was organized by the freezing of a small number of residues, equilibrium was reached via a large set of barrier crossings that correspond to backbone fluctuations. The heterogeneities inherent in structures gave rise to a distribution of side-chain relaxation times which spans more than an order of magnitude.

Original languageEnglish (US)
JournalPhysical Review Letters
Volume89
Issue number16
StatePublished - Oct 14 2002

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Protein Folding
folding
Freezing
proteins
freezing
relaxation time
simulation

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Medicine(all)

Cite this

Glassy dynamics of side-chain ordering in a simple model of protein folding. / Kussell, Edo; Shakhnovich, Eugene I.

In: Physical Review Letters, Vol. 89, No. 16, 14.10.2002.

Research output: Contribution to journalArticle

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