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