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dc.contributor.authorAhnert, Sebastian Edmunden
dc.contributor.authorMarsh, Joseph Aen
dc.contributor.authorHernández, Helenaen
dc.contributor.authorRobinson, Carol Ven
dc.contributor.authorTeichmann, Sarah Aen
dc.date.accessioned2015-12-04T14:46:21Z
dc.date.available2015-12-04T14:46:21Z
dc.date.issued2015-12-11en
dc.identifier.citationAhnert et al. Science (2015) Vol. 350 No. 6266, aaa2245. doi: 10.1126/science.aaa2245en
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/252861
dc.description.abstractStructural insights into protein complexes have had a broad impact on our understanding of biological function and evolution. Here we seek a comprehensive understanding of the general principles underlying quaternary structure organisation in protein complexes. To do this, we first examine the fundamental steps by which protein complexes can assemble using experimental and structure-based characterisation of assembly pathways. Most assembly transitions can be classified into three basic types, which can then be used to exhaustively enumerate a large set of possible quaternary structure topologies. These topologies, which include the vast majority of observed protein complex structures, give rise to a natural organisation into a periodic table. Based upon this, we are then able to accurately predict the expected frequencies of quaternary structure topologies, including those not yet observed. Overall, these results have important implications for quaternary structure prediction, modelling and engineering.
dc.description.sponsorshipThis work was supported by the Royal Society (S.E.A. and C.V.R.), the Human Frontier Science Program (J.A.M.), the Medical Research Council grant G1000819 (H.H. and C.V.R.) and the Lister Institute for Preventative Medicine (S.A.T.).
dc.languageEnglishen
dc.language.isoenen
dc.publisherAAAS
dc.titlePrinciples of assembly reveal a periodic table of protein complexesen
dc.typeArticle
dc.description.versionThis is the author accepted manuscript. The final version is available from AAAS via http://dx.doi.org/10.1126/science.aaa2245en
prism.numberaaa2245en
prism.publicationDate2015en
prism.publicationNameScienceen
prism.volume350en
dc.rioxxterms.funderMRC
dc.rioxxterms.projectidG1000819
rioxxterms.versionofrecord10.1126/science.aaa2245en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-12-11en
rioxxterms.typeJournal Article/Reviewen


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