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• W3099018255 abstract "In structure-based models of proteins, one often assumes that folding is accomplished when all contacts are established. This assumption may frequently lead to a conceptual problem that folding takes place in a temperature region of very low thermodynamic stability, especially when the contact map used is too sparse. We consider six different structure-based models and show that allowing for a small, but model-dependent, percentage of the native contacts not being established boosts the folding temperature substantially while affecting the time scales of folding only in a minor way. We also compare other properties of the six models. We show that the choice of the description of the backbone stiffness has a substantial effect on the values of characteristic temperatures that relate both to equilibrium and kinetic properties. Models without any backbone stiffness (like the self-organized polymer) are found to perform similar to those with the stiffness, including in the studies of stretching." @default.
• W3099018255 created "2020-11-23" @default.
• W3099018255 creator A5035656845 @default.
• W3099018255 creator A5040259634 @default.
• W3099018255 date "2016-05-13" @default.
• W3099018255 modified "2023-09-26" @default.
• W3099018255 title "Criteria for folding in structure-based models of proteins" @default.
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• W3099018255 doi "https://doi.org/10.1063/1.4948783" @default.
• W3099018255 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27179507" @default.
• W3099018255 hasPublicationYear "2016" @default.
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