Designable structures are easy to unfold

Cristiano L. Dias, Martin Grant

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


We study the structural stability of models of proteins for which the selected folds are unusually stable to mutation, that is, designable. A two-dimensional hydrophobic-polar lattice model was used to determine designable folds and these folds were investigated through Langevin dynamics. We find that the phase diagram of these proteins depends on their designability. In particular, highly designable folds are found to be weaker, i.e., easier to unfold, than low designable ones. We expect this to be related to protein flexibility.

Original languageEnglish (US)
Article number042902
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Issue number4
StatePublished - 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics


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