| Título: | Why Do Protein Folding Rates Correlate with Metrics ofNative Topology? |
| Autores: | Faísca, Patrícia F.N. ; Travasso, Rui D. M. ; Parisi, Andrea ; Rey Gayo, Antonio |
| Tipo de documento: | texto impreso |
| Editorial: | Public Library of Science, 2012-04-27 |
| Dimensiones: | application/pdf |
| Nota general: |
cc_by info:eu-repo/semantics/openAccess |
| Idiomas: | |
| Palabras clave: | Estado = Publicado , Materia = Ciencias: Química: Bioquímica , Materia = Ciencias: Química: Química física , Tipo = Artículo |
| Resumen: |
For almost 15 years, the experimental correlation between protein folding rates and the contact order parameter has been under scrutiny. Here, we use a simple simulation model combined with a native-centric interaction potential to investigate the physical roots of this empirical observation. We simulate a large set of circular permutants, thus eliminating dependencies of the folding rate on other protein properties (e.g. stability). We show that the rate-contact order correlation is a consequence of the fact that, in high contact order structures, the contact order of the transition state ensemble closely mirrors the contact order of the native state. This happens because, in these structures, the native topology is represented in the transition state through the formation of a network of tertiary interactions that are distinctively long-ranged. |
| En línea: | https://eprints.ucm.es/40935/1/PLoSOne_Faisca2012.pdf |
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