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Evolution of model proteins on a foldability landscape

dc.contributor.authorGovindarajan, Sridharen_US
dc.contributor.authorGoldstein, Richard A.en_US
dc.date.accessioned2006-04-28T17:02:36Z
dc.date.available2006-04-28T17:02:36Z
dc.date.issued1997-12en_US
dc.identifier.citationGovindarajan, Sridhar; Goldstein, Richard A. (1997)."Evolution of model proteins on a foldability landscape." Proteins: Structure, Function, and Genetics 29(4): 461-466. <http://hdl.handle.net/2027.42/38527>en_US
dc.identifier.issn0887-3585en_US
dc.identifier.issn1097-0134en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/38527
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9408943&dopt=citationen_US
dc.description.abstractWe model the evolution of simple lattice proteins as a random walk in a fitness landscape, where the fitness represents the ability of the protein to fold. At higher selective pressure, the evolutionary trajectories are confined to neutral networks where the native structure is conserved and the dynamics are non self-averaging and nonexponential. The optimizability of the corresponding native structure has a strong effect on the size of these neutral networks and thus on the nature of the evolutionary process. Proteins 29:461–466, 1997. © 1997 Wiley-Liss, Inc.en_US
dc.format.extent77847 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherChemistryen_US
dc.subject.otherBiochemistry and Biotechnologyen_US
dc.titleEvolution of model proteins on a foldability landscapeen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, Michiganen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan ; Biophysics Research Division, University of Michigan, Ann Arbor, Michigan ; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055en_US
dc.identifier.pmid9408943en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/38527/1/6_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/(SICI)1097-0134(199712)29:4<461::AID-PROT6>3.0.CO;2-Ben_US
dc.identifier.sourceProteins: Structure, Function, and Geneticsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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