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Influence of the native topology on the folding barrier for small proteins

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Prieto, Lidia and Rey, Antonio (2007) Influence of the native topology on the folding barrier for small proteins. The Journal of Chemical Physics, 127 . p. 175101. ISSN 0021-9606

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Official URL: https://aip.scitation.org/doi/10.1063/1.2780154




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.


Item Type:Article
Uncontrolled Keywords:Protein Folding | Proteins | folding mechanisms
Subjects:Sciences > Chemistry > Chemistry, Physical and theoretical
ID Code:49087
Deposited On:10 Dec 2018 12:48
Last Modified:10 Dec 2018 16:17

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