Why Do Protein Folding Rates Correlate with Metrics of Native Topology?
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 sim...
| Authors: | , , , |
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| Format: | article |
| Publication Date: | 2012 |
| Country: | España |
| Institution: | Universidad Complutense de Madrid (UCM) |
| Repository: | Docta Complutense |
| Language: | English |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/42591 |
| Online Access: | https://hdl.handle.net/20.500.14352/42591 |
| Access Level: | Open access |
| Keyword: | 544 article chemical structure chemistry computer simulation kinetics protein folding protein tertiary structure thermodynamics Bioquímica (Química) Química física (Química) |
| Summary: | 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. |
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