Folding nuclei in proteins

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

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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)708-717
Number of pages10
JournalMolekulyarnaya Biologiya
Issue number4
Publication statusPublished - 2001
Externally publishedYes


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