A surprising simplicity to protein folding

TitleA surprising simplicity to protein folding
Publication TypeJournal Article
Year of Publication2000
AuthorsBaker, D.
JournalNature
Volume405
Issue6782
Pagination39-42
Date Published2000 May 4
ISSN0028-0836
KeywordsAmino Acid Sequence, Models, Chemical, Models, Molecular, Peptides, Primary Publication, Protein Conformation, Protein Folding, Thermodynamics
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.

Alternate JournalNature
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