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SKEMPI 2.0: an updated benchmark of changes in protein–protein binding energy, kinetics and thermodynamics upon mutation

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10.1093/bioinformatics/bty635
 
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Cita com:
hdl:2117/123759

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Jankauskaite, Justina
Jiménez-García, Brian
Dapkunas, Justas
Fernández-Recio, Juan
Moal, Iain H.
Document typeArticle
Defense date2018-07-18
PublisherOxford University Press
Rights accessOpen Access
Attribution-NonCommercial-NoDerivs 4.0 Spain
Except where otherwise noted, content on this work is licensed under a Creative Commons license : Attribution-NonCommercial-NoDerivs 4.0 Spain
ProjectMuG - Multi-Scale Complex Genomics (EC-H2020-676556)
Abstract
Motivation: Understanding the relationship between the sequence, structure, binding energy, binding kinetics and binding thermodynamics of protein–protein interactions is crucial to understanding cellular signaling, the assembly and regulation of molecular complexes, the mechanisms through which mutations lead to disease, and protein engineering. Results: We present SKEMPI 2.0, a major update to our database of binding free energy changes upon mutation for structurally resolved protein–protein interactions. This version now contains manually curated binding data for 7085 mutations, an increase of 133%, including changes in kinetics for 1844 mutations, enthalpy and entropy changes for 443 mutations, and 440 mutations, which abolish detectable binding.
CitationJankauskaite, J. [et al.]. SKEMPI 2.0: an updated benchmark of changes in protein–protein binding energy, kinetics and thermodynamics upon mutation. "Bioinformatics", 18 Juliol 2018. 
URIhttp://hdl.handle.net/2117/123759
DOI10.1093/bioinformatics/bty635
ISSN1367-4803
Publisher versionhttps://academic.oup.com/bioinformatics/advance-article/doi/10.1093/bioinformatics/bty635/5055583
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