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dc.contributor.authorKolinski, Andrzej
dc.contributor.authorMilik, Mariusz
dc.contributor.authorSkolnick, Jeffrey
dc.date.accessioned2009-02-03T21:23:45Z
dc.date.available2009-02-03T21:23:45Z
dc.date.issued1991-03-01
dc.identifier.citationJournal of Chemical Physics, 1991:94: 3978-3985en
dc.identifier.issn0021-9606
dc.identifier.urihttp://hdl.handle.net/1853/26896
dc.description©1991 American Institute of Physicsen
dc.descriptionThe electronic version of this article is the complete one and can be found online at: http://link.aip.org/link/?JCPSA6/94/3978/1
dc.descriptionDOI:10.1063/1.460675
dc.description.abstractThe equilibrium and dynamic properties of a new lattice model of proteins are explored in the athermal limit. In this model, consecutive -carbons of the model polypeptide are connected by vectors of the type (±2,±1,0). In all cases, the chains have a finite backbone thickness which is close to that present in real proteins. Three different polypeptides are examined: polyglycine, polyalanine, and polyleucine. In the latter two cases, the side chains (whose conformations are extracted from known protein crystal structures) are included. For the equilibrium chain dimensions, with increasing side chain bulkiness, the effective chain length is smaller. The calculations suggest that these model polypeptides are in the same universality class as other polymer models. One surprising result is that although polyalanine and polyleucine have chiral sidechains, they do not induce a corresponding handedness of the main chain. For both polyleucine and polyalanine, the scaling of the self-diffusion constant and the terminal relaxation time are consistent with Rouse dynamics of excluded volume chains. Polyglycine exhibits a slightly stronger chain length dependence for these properties. This results from a finite length effect due to moderately long lived, local self-entanglements arising from the thin effective cross section of the chain backbone.en
dc.language.isoen_USen
dc.publisherGeorgia Institute of Technologyen
dc.subjectPolypeptidesen
dc.subjectChainsen
dc.subjectRelaxation timeen
dc.subjectProteinsen
dc.subjectGlycineen
dc.subjectAlaninesen
dc.subjectSelf-diffusionen
dc.subjectLattice dynamicsen
dc.titleStatic and dynamic properties of a new lattice model of polypeptide chainsen
dc.typeArticleen
dc.contributor.corporatenameResearch Institute of the Scripps Clinic. Dept. of Molecular Biology
dc.contributor.corporatenameUniwersytet Warszawski. Wydział Chemii
dc.publisher.originalAmerican Institute of Physics


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