DOI: 10.1073/pnas.87.9.3526. Metastability of the folded states of globular proteins.

Metastability of the folded states of globular proteins.

10.1073/pnas.87.9.3526

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

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.

Bibliography

Honeycutt, J. D., & Thirumalai, D. (1990). Metastability of the folded states of globular proteins. Proceedings of the National Academy of Sciences, 87(9), 3526â3529.

Authors 2

J D Honeycutt (first)
D Thirumalai (additional)

References 0 Referenced 272

None

Dates

Type	When
Created	19 years, 2 months ago (May 31, 2006, 7:38 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 1:05 p.m.)
Indexed	1 month ago (July 30, 2025, 11:26 a.m.)
Issued	35 years, 3 months ago (May 1, 1990)
Published	35 years, 3 months ago (May 1, 1990)
Published Online	35 years, 3 months ago (May 1, 1990)
Published Print	35 years, 3 months ago (May 1, 1990)

Funders 0

None

BibTeX

@article{Honeycutt_1990, title={Metastability of the folded states of globular proteins.}, volume={87}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.87.9.3526}, DOI={10.1073/pnas.87.9.3526}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Honeycutt, J D and Thirumalai, D}, year={1990}, month=may, pages={3526–3529} }

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