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• W1545810434 abstract "The growing structural coverage of proteomes is making structural comparison a powerful tool for function annotation. Such template-based approaches are based on the observation that structural similarity is often sufficient to infer similar function. However, it seems clear that, in addition to structural similarity, the specific characteristics of a given protein should also be taken into account in predicting function. Here we describe PredUs 2.0, a method to predict regions on a protein surface likely to bind other proteins, that is, interfacial residues. PredUs 2.0 is based on the PredUs method that is entirely template-based and uses known binding sites in structurally similar proteins to predict interfacial residues. PredUs 2.0 uses a Bayesian approach to combine the template-based scoring of PredUs with a score that reflects the propensities of individual amino acids to be in interfaces. PredUs 2.0 includes a novel protein size dependent metric to determine the number of residues that should be reported as interfacial. PredUs 2.0 significantly outperforms PredUs as well as other published interface prediction methods." @default.
• W1545810434 created "2016-06-24" @default.
• W1545810434 creator A5020269639 @default.
• W1545810434 creator A5036654109 @default.
• W1545810434 creator A5080456685 @default.
• W1545810434 date "2015-07-21" @default.
• W1545810434 modified "2023-09-27" @default.
• W1545810434 title "A hybrid method for protein-protein interface prediction" @default.
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• W1545810434 doi "https://doi.org/10.1002/pro.2744" @default.
• W1545810434 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4815308" @default.
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• W1545810434 hasPublicationYear "2015" @default.
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