Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families

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dc.citation.firstpageW233en_US
dc.citation.issueNumberW1en_US
dc.citation.journalTitleNucleic Acids Researchen_US
dc.citation.lastpageW237en_US
dc.citation.volumeNumber52en_US
dc.contributor.authorParra, R Gonzaloen_US
dc.contributor.authorFreiberger, Maria Ien_US
dc.contributor.authorPoley-Gil, Miriamen_US
dc.contributor.authorFernandez-Martin, Miguelen_US
dc.contributor.authorRadusky, Leandro Gen_US
dc.contributor.authorRuiz-Serra, Victoriaen_US
dc.contributor.authorWolynes, Peter Gen_US
dc.contributor.authorFerreiro, Diego Uen_US
dc.contributor.authorValencia, Alfonsoen_US
dc.contributor.orgCenter for Theoretical Biological Physicsen_US
dc.date.accessioned2024-08-09T16:25:25Zen_US
dc.date.available2024-08-09T16:25:25Zen_US
dc.date.issued2024en_US
dc.description.abstractAccording to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families.en_US
dc.identifier.citationParra, R. G., Freiberger, M. I., Poley-Gil, M., Fernandez-Martin, M., Radusky, L. G., Ruiz-Serra, V., Wolynes, P. G., Ferreiro, D. U., & Valencia, A. (2024). Frustraevo: A web server to localize and quantify the conservation of local energetic frustration in protein families. Nucleic Acids Research, 52(W1), W233–W237. https://doi.org/10.1093/nar/gkae244en_US
dc.identifier.digitalgkae244en_US
dc.identifier.doihttps://doi.org/10.1093/nar/gkae244en_US
dc.identifier.urihttps://hdl.handle.net/1911/117634en_US
dc.language.isoengen_US
dc.publisherOxford University Pressen_US
dc.rightsExcept where otherwise noted, this work is licensed under a Creative Commons Attribution-NonCommercial (CC BY-NC) license.  Permission to reuse, publish, or reproduce the work beyond the terms of the license or beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/en_US
dc.titleFrustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein familiesen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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