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- W2751993111 abstract "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." @default.
- W2751993111 created "2017-09-15" @default.
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- W2751993111 date "2005-03-21" @default.
- W2751993111 modified "2023-09-26" @default.
- W2751993111 title "Unfolding designable structures" @default.
- W2751993111 hasPublicationYear "2005" @default.
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