Unfolding designable structures

C. L. Dias, M. Grant

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Among an infinite number of possible folds, nature has chosen only about 1000 distinct folds to form protein structures. Theoretical studies suggest that selected folds are intrinsically more designable than others; these selected folds are unusually stable, a property called the designability principle. In this paper we use the 2D hydrophobic-polar lattice model to classify structures according to their designability, and Langevin dynamics to account for their time evolution in the presence of shear flow. We demonstrate that, among all possible folds, the more designable ones are easier to unfold due to their large number of surface-core bonds.

Original languageEnglish (US)
Pages (from-to)265-269
Number of pages5
JournalEuropean Physical Journal B
Issue number1-2
StatePublished - Mar 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics


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