{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T08:26:23Z","timestamp":1775291183977,"version":"3.50.1"},"reference-count":19,"publisher":"Oxford University Press (OUP)","issue":"18","license":[{"start":{"date-parts":[[2021,3,15]],"date-time":"2021-03-15T00:00:00Z","timestamp":1615766400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000001","name":"NSF","doi-asserted-by":"publisher","award":["PHY-2019745"],"award-info":[{"award-number":["PHY-2019745"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007863","name":"Rice University","doi-asserted-by":"publisher","award":["C-0016"],"award-info":[{"award-number":["C-0016"]}],"id":[{"id":"10.13039\/100007863","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,9,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Summary<\/jats:title>\n                    <jats:p>Once folded, natural protein molecules have few energetic conflicts within their polypeptide chains. Many protein structures do however contain regions where energetic conflicts remain after folding, i.e. they are highly frustrated. These regions, kept in place over evolutionary and physiological timescales, are related to several functional aspects of natural proteins such as protein\u2013protein interactions, small ligand recognition, catalytic sites and allostery. Here, we present FrustratometeR, an R package that easily computes local energetic frustration on a personal computer or a cluster. This package facilitates large scale analysis of local frustration, point mutants and molecular dynamics (MD) trajectories, allowing straightforward integration of local frustration analysis into pipelines for protein structural analysis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Availability and implementation<\/jats:title>\n                    <jats:p>https:\/\/github.com\/proteinphysiologylab\/frustratometeR.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Supplementary information<\/jats:title>\n                    <jats:p>Supplementary data are available at Bioinformatics online.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btab176","type":"journal-article","created":{"date-parts":[[2021,3,11]],"date-time":"2021-03-11T15:11:15Z","timestamp":1615475475000},"page":"3038-3040","source":"Crossref","is-referenced-by-count":55,"title":["FrustratometeR: an R-package to compute local frustration in protein structures, point mutants and MD simulations"],"prefix":"10.1093","volume":"37","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6769-2510","authenticated-orcid":false,"given":"Atilio O","family":"Rausch","sequence":"first","affiliation":[{"name":"Facultad de Ingenier\u00eda, Universidad Nacional de Entre R\u00edos , Entre R\u00edos E3100XAD, Argentina"}]},{"given":"Maria I","family":"Freiberger","sequence":"additional","affiliation":[{"name":"Laboratorio de Fisiolog\u00eda de Prote\u00ednas, Departamento de Qu\u00edmica Biol\u00f3gica \u2013 IQUIBICEN\/CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires , Buenos Aires C1428EGA, Argentina"}]},{"given":"Cesar O","family":"Leonetti","sequence":"additional","affiliation":[{"name":"Laboratorio de Fisiolog\u00eda de Prote\u00ednas, Departamento de Qu\u00edmica Biol\u00f3gica \u2013 IQUIBICEN\/CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires , Buenos Aires C1428EGA, Argentina"}]},{"given":"Diego M","family":"Luna","sequence":"additional","affiliation":[{"name":"Facultad de Ingenier\u00eda, Universidad Nacional de Entre R\u00edos , Entre R\u00edos E3100XAD, Argentina"}]},{"given":"Leandro G","family":"Radusky","sequence":"additional","affiliation":[{"name":"Center for Genomic Regulation, Barcelona Institute for Science and Technology , Barcelona 08003, Spain"}]},{"given":"Peter G","family":"Wolynes","sequence":"additional","affiliation":[{"name":"Center for Theoretical Biological Physics and Department of Chemistry, Rice University , Houston, TX 77005, USA"}]},{"given":"Diego U","family":"Ferreiro","sequence":"additional","affiliation":[{"name":"Laboratorio de Fisiolog\u00eda de Prote\u00ednas, Departamento de Qu\u00edmica Biol\u00f3gica \u2013 IQUIBICEN\/CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires , Buenos Aires C1428EGA, Argentina"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2446-016X","authenticated-orcid":false,"given":"R Gonzalo","family":"Parra","sequence":"additional","affiliation":[{"name":"Genome Biology Unit, European Molecular Biology Laboratory , Heidelberg 69117, Germany"}]}],"member":"286","published-online":{"date-parts":[[2021,3,15]]},"reference":[{"key":"2023061402422289100_btab176-B1","doi-asserted-by":"crossref","first-page":"7524","DOI":"10.1073\/pnas.84.21.7524","article-title":"Spin glasses and the statistical mechanics of protein folding","volume":"84","author":"Bryngelson","year":"1987","journal-title":"Proc. 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