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dc.contributor.authorDąbrowski-Tumański, Paweł-
dc.contributor.authorJarmolińska, Aleksandra I.-
dc.contributor.authorNiemyska, Wanda-
dc.contributor.authorRawdon, Eric J.-
dc.contributor.authorMillett, Kenneth C.-
dc.contributor.authorSułkowska, Joanna I.-
dc.date.accessioned2018-05-24T11:32:16Z-
dc.date.available2018-05-24T11:32:16Z-
dc.date.issued2017-
dc.identifier.citationNucleic Acids Research, Vol. 45, iss. D1 (2017), s. D243-D249pl_PL
dc.identifier.issn0305-1048-
dc.identifier.urihttp://hdl.handle.net/20.500.12128/3965-
dc.description.abstractProtein chains are known to fold into topologically complex shapes, such as knots, slipknots or complex lassos. This complex topology of the chain can be considered as an additional feature of a protein, separate from secondary and tertiary structures. Moreover, the complex topology can be defined also as one additional structural level. The LinkProt database (http://linkprot.cent.uw.edu.pl) collects and displays information about protein links - topologically non-trivial structures made by up to four chains and complexes of chains (e.g. in capsids). The database presents deterministic links (with loops closed, e.g. by two disulfide bonds), links formed probabilistically and macromolecular links. The structures are classified according to their topology and presented using the minimal surface area method. The database is also equipped with basic tools which allow users to analyze the topology of arbitrary (bio)polymers.pl_PL
dc.language.isoenpl_PL
dc.relation1418869, 0003/ID3/2016, 2057, 2012/07/E/NZ1/01900, 130/UD/SKILLS/2015, 120000-501/86-DSM-112 700pl_PL
dc.rightsUznanie autorstwa 3.0 Polska*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/pl/*
dc.subjectLinkProtpl_PL
dc.subjectdatabasepl_PL
dc.subjectinformation processingpl_PL
dc.titleLinkProt : a database collecting information about biological linkspl_PL
dc.typeinfo:eu-repo/semantics/articlepl_PL
dc.identifier.doi10.1093/nar/gkw976-
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Uznanie Autorstwa 3.0 Polska Creative Commons Creative Commons