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Article

Functional effects of mutations in proteins can be predicted and interpreted by guided selection of sequence covariation information.

Proceedings of the National Academy of Sciences of the United States of America - 25 Jun 2024

Cocco Simona, Posani Lorenzo, Monasson Rémi

Abstract excerpt

Predicting the effects of one or more mutations to the in vivo or in vitro properties of a wild-type protein is a major computational challenge, due to the presence of epistasis, that is, of interactions between amino acids in the sequence. We introduce a computationally efficient procedure to build minimal epistatic models to predict mutational effects by combining evolutionary (homologous sequence) and few...

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Identifiers

PMID: 38889151
DOI: 10.1073/pnas.2312335121
PMCID: PMC11214004

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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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