{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,13]],"date-time":"2025-11-13T12:16:39Z","timestamp":1763036199745},"reference-count":12,"publisher":"Oxford University Press (OUP)","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2007,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Summary: SMotif is a server that identifies important structural segments or motifs for a given protein structure(s) based on conservation of both sequential as well as important structural features such as solvent inaccessibility, secondary structural content, hydrogen bonding pattern and residue packing. This server also provides three-dimensional orientation patterns of the identified motifs in terms of inter-motif distances and torsion angles. These motifs may form the common core and therefore, can also be employed to design and rationalize protein engineering and folding experiments.<\/jats:p><jats:p>Availability: SMotif server is available via the URL http:\/\/caps.ncbs.res.in\/SMotif\/index.html.<\/jats:p><jats:p>Contact: \u00a0chakraba@mail.nih.gov, mini@ncbs.res.in or EPNSugan@ntu.edu.sg<\/jats:p><jats:p>Supplementary information: Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btl679","type":"journal-article","created":{"date-parts":[[2007,1,20]],"date-time":"2007-01-20T01:12:50Z","timestamp":1169255570000},"page":"637-638","source":"Crossref","is-referenced-by-count":16,"title":["SMotif: a server for structural motifs in proteins"],"prefix":"10.1093","volume":"23","author":[{"given":"Ganesan","family":"Pugalenthi","sequence":"first","affiliation":[{"name":"1 School of Electrical and Electronic Engineering, Nanyang Technological University, Singapore 639798, 2National Centre for Biological Sciences, Bangalore 560 065, India and 3National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P. N.","family":"Suganthan","sequence":"additional","affiliation":[{"name":"1 School of Electrical and Electronic Engineering, Nanyang Technological University, Singapore 639798, 2National Centre for Biological Sciences, Bangalore 560 065, India and 3National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Sowdhamini","sequence":"additional","affiliation":[{"name":"1 School of Electrical and Electronic Engineering, Nanyang Technological University, Singapore 639798, 2National Centre for Biological Sciences, Bangalore 560 065, India and 3National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saikat","family":"Chakrabarti","sequence":"additional","affiliation":[{"name":"1 School of Electrical and Electronic Engineering, Nanyang Technological University, Singapore 639798, 2National Centre for Biological Sciences, Bangalore 560 065, India and 3National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2007,1,19]]},"reference":[{"key":"2023041109374573000_","first-page":"33","article-title":"Protein sequence annotation in the genome era: the annotation concept of SWISS-PROT, TREMBL","author":"Apweiler","year":"1997"},{"key":"2023041109374573000_","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2023041109374573000_","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":"2023041109374573000_","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.febslet.2004.05.028","article-title":"Regions of minimal structural variation among members of protein domain superfamilies: application to remote homology detection and modeling using distant relationships","volume":"569","author":"Chakrabarti","year":"2004","journal-title":"FEBS Lett."},{"key":"2023041109374573000_","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1093\/protein\/gzg110","article-title":"SMoS: a database of structural motifs of protein superfamilies","volume":"16","author":"Chakrabarti","year":"2003","journal-title":"Protein Eng."},{"key":"2023041109374573000_","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/0968-0004(90)90035-A","article-title":"The evolution of alpha\/beta barrel enzymes","volume":"15","author":"Farber","year":"1990","journal-title":"Trends Biochem. 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