Evolution of model proteins on a foldability landscape
dc.contributor.author | Govindarajan, Sridhar | en_US |
dc.contributor.author | Goldstein, Richard A. | en_US |
dc.date.accessioned | 2006-04-28T17:02:36Z | |
dc.date.available | 2006-04-28T17:02:36Z | |
dc.date.issued | 1997-12 | en_US |
dc.identifier.citation | Govindarajan, 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.issn | 0887-3585 | en_US |
dc.identifier.issn | 1097-0134 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38527 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9408943&dopt=citation | en_US |
dc.description.abstract | We 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.extent | 77847 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Biochemistry and Biotechnology | en_US |
dc.title | Evolution of model proteins on a foldability landscape | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationum | Department 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 48109-1055 | en_US |
dc.identifier.pmid | 9408943 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38527/1/6_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/(SICI)1097-0134(199712)29:4<461::AID-PROT6>3.0.CO;2-B | en_US |
dc.identifier.source | Proteins: Structure, Function, and Genetics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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