Phys Rev E Stat Nonlin Soft Matter Phys. 2006 Oct;74(4 Pt 1):042902. Epub 2006 Oct 9.

Designable structures are easy to unfold.

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Physics Department, Rutherford Building, McGill University, 3600 rue University, Montréal, Québec H3A 2T8, Canada.

Abstract

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.

PMID:: 17155116; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

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Proteins

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Cited by 1 PubMed Central article

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