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• W1989756489 abstract "The possibility of downhill instead of two-state folding for proteins has been a very controversial topic which arose from recent experimental studies. From the theoretical side, this question has also been accomplished in different ways. Given the experimental observation that a relationship exists between the native structure topology of a protein and the kinetic and thermodynamic properties of its folding process, Gō-type potentials are an appropriate way to approach this problem. In this work, we employ an interaction potential from this family to get a better insight on the topological characteristics of the native state that may somehow determine the presence of a thermodynamic barrier in the folding pathway. The results presented here show that, indeed, the native topology of a small protein has a great influence on its folding behavior, mostly depending on the proportion of local and long range contacts the protein has in its native structure. Furthermore, when all the interactions present contribute in a balanced way, the transition results to be cooperative. Otherwise, the tendency to a downhill folding behavior increases." @default.
• W1989756489 created "2016-06-24" @default.
• W1989756489 creator A5032129884 @default.
• W1989756489 creator A5032889484 @default.
• W1989756489 date "2007-11-02" @default.
• W1989756489 modified "2023-09-30" @default.
• W1989756489 title "Influence of the native topology on the folding barrier for small proteins" @default.
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• W1989756489 doi "https://doi.org/10.1063/1.2780154" @default.
• W1989756489 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17994851" @default.
• W1989756489 hasPublicationYear "2007" @default.
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