{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,25]],"date-time":"2026-01-25T04:39:10Z","timestamp":1769315950449,"version":"3.49.0"},"reference-count":11,"publisher":"Oxford University Press (OUP)","issue":"20","license":[{"start":{"date-parts":[[2016,10,2]],"date-time":"2016-10-02T00:00:00Z","timestamp":1475366400000},"content-version":"vor","delay-in-days":2231,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.0\/uk\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,10,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary: The defined secondary structure of proteins method is often considered the gold standard for assignment of secondary structure from three-dimensional coordinates. However, there are alternative methods. \u20182Struc: The Secondary Structure Server\u2019 has been created as a single point of access for eight different secondary structure assignment methods. It has been designed to enable comparisons between methods for analyzing the secondary structure content for a single protein. It also includes a second functionality, \u2018Compare-the-Protein\u2019 to enable comparisons of the secondary structure features from any one method to be made within a collection of nuclear magnetic resonance models, or between the crystal structures of two different proteins.<\/jats:p>\n               <jats:p>Availability: \u00a0http:\/\/2struc.cryst.bbk.ac.uk<\/jats:p>\n               <jats:p>Contact: \u00a0r.w.janes@qmul.ac.uk<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btq480","type":"journal-article","created":{"date-parts":[[2010,8,26]],"date-time":"2010-08-26T00:33:02Z","timestamp":1282782782000},"page":"2624-2625","source":"Crossref","is-referenced-by-count":122,"title":["2Struc: the secondary structure server"],"prefix":"10.1093","volume":"26","author":[{"given":"D. P.","family":"Klose","sequence":"first","affiliation":[{"name":"1 School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS and 2Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK"}]},{"given":"B. A.","family":"Wallace","sequence":"additional","affiliation":[{"name":"1 School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS and 2Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK"}]},{"given":"Robert W.","family":"Janes","sequence":"additional","affiliation":[{"name":"1 School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS and 2Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK"}]}],"member":"286","published-online":{"date-parts":[[2010,8,24]]},"reference":[{"key":"2023012507561793400_B1","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0969-2126(02)00700-1","article-title":"Continuum secondary structure captures protein flexibility","volume":"10","author":"Anderson","year":"2002","journal-title":"Structure"},{"key":"2023012507561793400_B2","doi-asserted-by":"crossref","first-page":"D301","DOI":"10.1093\/nar\/gkl971","article-title":"The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data","volume":"35","author":"Berman","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2023012507561793400_B3","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1002\/prot.340230412","article-title":"Knowledge-based protein secondary structure assignment","volume":"23","author":"Frishman","year":"1995","journal-title":"Proteins Struct. 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