Symmetry and designability for lattice protein models

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

Research output: Contribution to journalArticle

33 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 languageEnglish (US)
Pages (from-to)8329-8336
Number of pages8
JournalJournal of Chemical Physics
Volume113
Issue number18
DOIs
StatePublished - Nov 8 2000

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Fingerprint Dive into the research topics of 'Symmetry and designability for lattice protein models'. Together they form a unique fingerprint.

  • Cite this