Metastability of the folded states of globular proteins.

Honeycutt, J D; Thirumalai, D · Proc Natl Acad Sci U S A · 1990

basic_science · Level V

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Abstract

The possibility that several metastable minima exist in which the folded forms of a polypeptide chain have similar structural characteristics but different energies is suggested. The validity of this hypothesis is illustrated with the aid of simulation methods on a model protein that folds into a beta-barrel structure. Some implications of this hypothesis such as the existence of multiple pathways with intermediates for protein folding are discussed.

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