Symmetry and designability for lattice protein models

Tairan Wang; Jonathan Miller; Ned S. Wingreen; Chao Tang; Ken A. Dill

doi:10.1063/1.1315324

Symmetry and designability for lattice protein models

Tairan Wang, Jonathan Miller, Ned S. Wingreen, Chao Tang, Ken A. Dill

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

Relationship between the symmetries of native proteins and their designabilities was studied. Native structures encoded by different sequences were found to have high symmetry. The study was done using a two-dimensional lattice protein model based on hydrophobicity.

Original language	English (US)
Pages (from-to)	8329-8336
Number of pages	8
Journal	Journal of Chemical Physics
Volume	113
Issue number	18
DOIs	https://doi.org/10.1063/1.1315324
State	Published - Nov 8 2000

All Science Journal Classification (ASJC) codes

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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10.1063/1.1315324

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title = "Symmetry and designability for lattice protein models",

abstract = "Relationship between the symmetries of native proteins and their designabilities was studied. Native structures encoded by different sequences were found to have high symmetry. The study was done using a two-dimensional lattice protein model based on hydrophobicity.",

author = "Tairan Wang and Jonathan Miller and Wingreen, {Ned S.} and Chao Tang and Dill, {Ken A.}",

year = "2000",

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T1 - Symmetry and designability for lattice protein models

AU - Wang, Tairan

AU - Miller, Jonathan

AU - Wingreen, Ned S.

AU - Tang, Chao

AU - Dill, Ken A.

PY - 2000/11/8

Y1 - 2000/11/8

N2 - Relationship between the symmetries of native proteins and their designabilities was studied. Native structures encoded by different sequences were found to have high symmetry. The study was done using a two-dimensional lattice protein model based on hydrophobicity.

AB - Relationship between the symmetries of native proteins and their designabilities was studied. Native structures encoded by different sequences were found to have high symmetry. The study was done using a two-dimensional lattice protein model based on hydrophobicity.

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U2 - 10.1063/1.1315324

DO - 10.1063/1.1315324

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JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 18

ER -

Symmetry and designability for lattice protein models

Abstract

All Science Journal Classification (ASJC) codes

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