Computer simulation of protein folding.

Nature ·Vol. 253 ·No. 5494 ·1975-02-27 ·Pages 694-8

Levitt M, Warshel A

Abstract

A new and very simple representation of protein conformations has been used together with energy minimisation and thermalisation to simulate protein folding. Under certain conditions, the method succeeds in "renaturing" bovine pancreatic trypsin inhibitor from an open-chain conformation into a folded conformation close to that of the native molecule.

MeSH Terms

Amino Acid Sequence Animals Cattle Computers Models, Chemical Models, Molecular Protein Conformation Trypsin Inhibitors

Chemicals

Trypsin Inhibitors

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Levitt M

Warshel A

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/253694a0

Published

1975-02-27

Pages

694-8

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/253694a0 View journal details

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Computer simulation of protein folding.

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