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PMID: 10811210 Published · ppublish English Journal Article

A surprising simplicity to protein folding.

Nature ·Vol. 405 ·No. 6782 ·2000-05-04 ·Pages 39-42

Baker D

Abstract

The polypeptide chains that make up proteins have thousands of atoms and hence millions of possible inter-atomic interactions. It might be supposed that the resulting complexity would make prediction of protein structure and protein-folding mechanisms nearly impossible. But the fundamental physics underlying folding may be much simpler than this complexity would lead us to expect folding rates and mechanisms appear to be largely determined by the topology of the native (folded) state, and new methods have shown great promise in predicting protein-folding mechanisms and the three-dimensional structures of proteins.

MeSH Terms
Amino Acid Sequence Models, Chemical Models, Molecular Peptides/chemistry Protein Conformation Protein Folding Thermodynamics
Chemicals
Peptides
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Baker D
Department of Biochemistry, University of Washington, Seattle 98195, USA.
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
2000-05-04
Pages
39-42
Language
English
Region
England
NLM ID
0410462
Subset
IM
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