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Article

Proposed mechanism for stability of proteins to evolutionary mutations.

Proceedings of the National Academy of Sciences of the United States of America - 1 Sept 1998

Nelson E D, Onuchic J N

Abstract excerpt

It is shown that the sequence-ordering tendencies induced by design into different fast-folding, thermally stable native structures interfere. This interference results in a type of quasiorthogonality between optimal native structures, which divides sequence space into fast-folding, thermally stable families surrounded by slow-folding, low stability shells. A concrete example of this effect is provided by using a...

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Identifiers

PMID: 9724764
DOI: 10.1073/pnas.95.18.10682
PMCID: PMC27955

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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