Designable structures are easy to unfold.

Cristiano L Dias; Martin Grant

doi:10.1103/physreve.74.042902

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Designable structures are easy to unfold.

Cristiano L Dias·Martin Grant

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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.

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Amino Acid Sequence Computer Simulation Drug Design Models, Chemical Models, Molecular Molecular Sequence Data Protein Conformation Protein Denaturation Protein Folding Proteins Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't

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Cristiano L Dias, Martin Grant. 2006-10-09. Designable structures are easy to unfold.. https://doi.org/10.1103/physreve.74.042902

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