Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.

doi:10.1006/jmbi.1999.2911

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Article

Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.

Journal of molecular biology - 6 Aug 1999

Mirny L A, Shakhnovich E I

Abstract excerpt

Here, we provide an analysis of molecular evolution of five of the most populated protein folds: immunoglobulin fold, oligonucleotide-binding fold, Rossman fold, alpha/beta plait, and TIM barrels. In order to distinguish between "historic", functional and structural reasons for amino acid conservations, we consider proteins that acquire the same fold and have no evident sequence homology. For each fold we...

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PMID: 10438614
DOI: 10.1006/jmbi.1999.2911

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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