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"New view" of protein folding reconciled with the old through multiple unfolding simulations.

Authors
  • Lazaridis, T
  • Karplus, M
Type
Published Article
Journal
Science (New York, N.Y.)
Publication Date
Dec 12, 1997
Volume
278
Issue
5345
Pages
1928–1931
Identifiers
PMID: 9395391
Source
Medline
License
Unknown

Abstract

Twenty-four molecular dynamics trajectories of chymotrypsin inhibitor 2 provide a direct demonstration of the diversity of unfolding pathways. Comparison with experiments suggests that the transition state region for folding and unfolding occurs early with only 25 percent of the native contacts and that the root-mean-square deviations between contributing structures can be as large as 15 angstroms. Nevertheless, a statistically preferred unfolding pathway emerges from the simulations; disruption of tertiary interactions between the helix and a two-stranded portion of the beta sheet is the primary unfolding event. The results suggest a synthesis of the "new" and the classical view of protein folding with a preferred pathway on a funnel-like average energy surface.

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