{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,11]],"date-time":"2026-04-11T13:47:26Z","timestamp":1775915246664,"version":"3.50.1"},"reference-count":36,"publisher":"Oxford University Press (OUP)","issue":"14","license":[{"start":{"date-parts":[[2021,1,20]],"date-time":"2021-01-20T00:00:00Z","timestamp":1611100800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"F.R.S.-FNRS Fund for Scientific Research"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,8,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Motivation<\/jats:title>\n                    <jats:p>Although structured proteins adopt their lowest free energy conformation in physiological conditions, the individual residues are generally not in their lowest free energy conformation. Residues that are stability weaknesses are often involved in functional regions, whereas stability strengths ensure local structural stability. The detection of strengths and weaknesses provides key information to guide protein engineering experiments aiming to modulate folding and various functional processes.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>We developed the SWOTein predictor which identifies strong and weak residues in proteins on the basis of three types of statistical energy functions describing local interactions along the chain, hydrophobic forces and tertiary interactions. The large-scale analysis of the different types of strengths and weaknesses demonstrated their complementarity and the enhancement of the information they provide. Moreover, a good average correlation was observed between predicted and experimental strengths and weaknesses obtained from native hydrogen exchange data. SWOTein application to three test cases further showed its suitability to predict and interpret strong and weak residues in the context of folding, conformational changes and protein-protein binding. In summary, SWOTein is both fast and accurate and can be applied at small and large scale to analyze and modulate folding and molecular recognition processes.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Availabilityand implementation<\/jats:title>\n                    <jats:p>The SWOTein webserver provides the list of predicted strengths and weaknesses and a protein structure visualization tool that facilitates the interpretation of the predictions. It is freely available for academic use at http:\/\/babylone.ulb.ac.be\/SWOTein\/.<\/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\/btab034","type":"journal-article","created":{"date-parts":[[2021,1,15]],"date-time":"2021-01-15T15:33:31Z","timestamp":1610724811000},"page":"1963-1971","source":"Crossref","is-referenced-by-count":22,"title":["SWOTein: a structure-based approach to predict stability Strengths and Weaknesses of prOTEINs"],"prefix":"10.1093","volume":"37","author":[{"given":"Qingzhen","family":"Hou","sequence":"first","affiliation":[{"name":"Department of Biostatistics, School of Public Health, Cheeloo College of Medicine, Shandong University , Shandong 250002, China"},{"name":"National Institute of Health Data Science of China, Shandong University , Shandong 250002, China"},{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2916-022X","authenticated-orcid":false,"given":"Fabrizio","family":"Pucci","sequence":"additional","affiliation":[{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"},{"name":"Interuniversity Institute of Bioinformatics in Brussels, Boulevard du Triomphe , Brussels 1050, Belgium"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0895-1746","authenticated-orcid":false,"given":"Fran\u00e7ois","family":"Ancien","sequence":"additional","affiliation":[{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"},{"name":"Interuniversity Institute of Bioinformatics in Brussels, Boulevard du Triomphe , Brussels 1050, Belgium"}]},{"given":"Jean Marc","family":"Kwasigroch","sequence":"additional","affiliation":[{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"}]},{"given":"Rapha\u00ebl","family":"Bourgeas","sequence":"additional","affiliation":[{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"}]},{"given":"Marianne","family":"Rooman","sequence":"additional","affiliation":[{"name":"Department of Computational Biology and Bioinformatics, Universit\u00e9 Libre de Bruxelles , Brussels 1050, Belgium"},{"name":"Interuniversity Institute of Bioinformatics in Brussels, Boulevard du Triomphe , Brussels 1050, Belgium"}]}],"member":"286","published-online":{"date-parts":[[2021,1,20]]},"reference":[{"key":"2023061310290819700_btab034-B1","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/S0968-0004(98)01346-2","article-title":"Is protein folding hierarchic? 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