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Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site.

par Wainreb, Gilad;Wolf, Lior;Ashkenazy, Haim;Dehouck, Yves ;Ben-Tal, Nir
Référence Bioinformatics, 27, 23, page (3286-3292)
Publication Publié, 2011-12

Article révisé par les pairs

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Résumé :

Accurate prediction of protein stability is important for understanding the molecular underpinnings of diseases and for the design of new proteins. We introduce a novel approach for the prediction of changes in protein stability that arise from a single-site amino acid substitution; the approach uses available data on mutations occurring in the same position and in other positions. Our algorithm, named Pro-Maya (Protein Mutant stAbilitY Analyzer), combines a collaborative filtering baseline model, Random Forests regression and a diverse set of features. Pro-Maya predicts the stability free energy difference of mutant versus wild type, denoted as ΔΔG.