Static and dynamic properties of a new lattice model of polypeptide chains

dc.contributor.author Kolinski, Andrzej
dc.contributor.author Milik, Mariusz
dc.contributor.author Skolnick, Jeffrey
dc.contributor.corporatename Research Institute of the Scripps Clinic. Dept. of Molecular Biology
dc.contributor.corporatename Uniwersytet Warszawski. Wydział Chemii
dc.date.accessioned 2009-02-03T21:23:45Z
dc.date.available 2009-02-03T21:23:45Z
dc.date.issued 1991-03-01
dc.description ©1991 American Institute of Physics en
dc.description The 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.description DOI:10.1063/1.460675
dc.description.abstract The 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.identifier.citation Journal of Chemical Physics, 1991:94: 3978-3985 en
dc.identifier.issn 0021-9606
dc.identifier.uri http://hdl.handle.net/1853/26896
dc.language.iso en_US en
dc.publisher Georgia Institute of Technology en
dc.publisher.original American Institute of Physics
dc.subject Polypeptides en
dc.subject Chains en
dc.subject Relaxation time en
dc.subject Proteins en
dc.subject Glycine en
dc.subject Alanines en
dc.subject Self-diffusion en
dc.subject Lattice dynamics en
dc.title Static and dynamic properties of a new lattice model of polypeptide chains en
dc.type Text
dc.type.genre Article
dspace.entity.type Publication
local.contributor.author Skolnick, Jeffrey
local.contributor.corporatename College of Sciences
local.contributor.corporatename School of Biological Sciences
local.contributor.corporatename Center for the Study of Systems Biology
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