{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T01:38:07Z","timestamp":1774402687675,"version":"3.50.1"},"reference-count":39,"publisher":"Oxford University Press (OUP)","issue":"21","license":[{"start":{"date-parts":[[2017,6,26]],"date-time":"2017-06-26T00:00:00Z","timestamp":1498435200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"funder":[{"DOI":"10.13039\/501100002661","name":"FNRS","doi-asserted-by":"publisher","award":["T.0100.16"],"award-info":[{"award-number":["T.0100.16"]}],"id":[{"id":"10.13039\/501100002661","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>The molecular bases of protein stability remain far from elucidated even though substantial progress has been made through both computational and experimental investigations. One of the most challenging goals is the development of accurate prediction tools of the temperature dependence of the standard folding free energy \u0394G(T). Such predictors have an enormous series of potential applications, which range from drug design in the biopharmaceutical sector to the optimization of enzyme activity for biofuel production. There is thus an important demand for novel, reliable and fast predictors.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>We present the SCooP algorithm, which is a significant step towards accurate temperature-dependent stability prediction. This automated tool uses the protein structure and the host organism as sole entries and predicts the full T-dependent stability curve of monomeric proteins assumed to follow a two-state folding transition. Equivalently, it predicts all the thermodynamic quantities associated to the folding transition, namely the melting temperature Tm, the standard folding enthalpy \u0394Hm measured at Tm, and the standard folding heat capacity \u0394Cp. The cross-validated performances are good, with correlation coefficients between predicted and experimental values equal to [0.80, 0.83, 0.72] for \u0394Hm, \u0394Cp and Tm, respectively, which increase up to [0.88, 0.90, 0.78] upon the removal of 10% outliers. Moreover, the stability curve prediction of a target protein is very fast: it takes less than a minute. SCooP can thus potentially be applied on a structurome scale. This opens new perspectives of large-scale analyses of protein stability, which is of considerable interest for protein engineering.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>The SCooP webserver is freely available at http:\/\/babylone.ulb.ac.be\/SCooP.<\/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\/btx417","type":"journal-article","created":{"date-parts":[[2017,6,23]],"date-time":"2017-06-23T11:25:10Z","timestamp":1498217110000},"page":"3415-3422","source":"Crossref","is-referenced-by-count":101,"title":["SCooP: an accurate and fast predictor of protein stability curves as a function of temperature"],"prefix":"10.1093","volume":"33","author":[{"given":"Fabrizio","family":"Pucci","sequence":"first","affiliation":[{"name":"Department of BioModeling BioInformatics and BioProcesses, Universit\u00e9 Libre de Bruxelles and Interuniversity Institute of Bioinformatics in Brussels, Triumph Bld, Brussels, Belgium"}]},{"given":"Jean Marc","family":"Kwasigroch","sequence":"additional","affiliation":[{"name":"Department of BioModeling BioInformatics and BioProcesses, Universit\u00e9 Libre de Bruxelles and Interuniversity Institute of Bioinformatics in Brussels, Triumph Bld, Brussels, Belgium"}]},{"given":"Marianne","family":"Rooman","sequence":"additional","affiliation":[{"name":"Department of BioModeling BioInformatics and BioProcesses, Universit\u00e9 Libre de Bruxelles and Interuniversity Institute of Bioinformatics in Brussels, Triumph Bld, Brussels, Belgium"}]}],"member":"286","published-online":{"date-parts":[[2017,6,26]]},"reference":[{"key":"2023051506353360300_btx417-B1","doi-asserted-by":"crossref","first-page":"365","DOI":"10.2976\/1.2991513","article-title":"Studying the folding of multidomain proteins","volume":"2","author":"Batey","year":"2008","journal-title":"HFSP J"},{"key":"2023051506353360300_btx417-B2","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The protein data bank","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res"},{"key":"2023051506353360300_btx417-B3","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1385\/ABAB:90:2:155","article-title":"Thermozymes and their applications","volume":"90","author":"Bruins","year":"2001","journal-title":"Appl. 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