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Folding nuclei in proteins
Author(s) -
Galzitskaya Oxana V,
Ivankov Dmitry N,
Finkelstein Alexei V
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02092-0
Subject(s) - metastability , folding (dsp implementation) , folding funnel , protein folding , downhill folding , phi value analysis , chemistry , kinetics , contact order , native state , chemical physics , biophysics , crystallography , physics , biology , classical mechanics , biochemistry , organic chemistry , electrical engineering , engineering
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 just close to 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. Our aim is to review recent experimental and theoretical studies of the folding nuclei.