Folding nuclei in proteins

O. V. Galzitskaya, D. N. Ivankov, A. V. Finkelstein

Research output: Contribution to journalReview articlepeer-review

3 Citations (Scopus)

Abstract

When a protein folds or unfolds, it passes through many half-folded microstates. Only a few of them can accumulate and be seen experimentally, and this happens only when the folding (or unfolding) occurs far from the point of thermodynamic equilibrium between the native and denatured states. The universal features of folding, though, are observed in the vicinity of the equilibrium point. Here the two-state transition proceeds without any accumulation of metastable intermediates, and only the transition state (folding nucleus) is outlined by its key influence on the folding/unfolding kinetics. This review covers recent experimental and theoretical studies of folding nuclei.

Original languageEnglish
Pages (from-to)605-613
Number of pages9
JournalMolecular Biology
Volume35
Issue number4
DOIs
Publication statusPublished - Jul 2001
Externally publishedYes

Keywords

  • All-or-none transition
  • Folding intermediates
  • Folding nucleus
  • Protein folding
  • Rate of folding
  • Transition state
  • Two-state kinetics

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