Loop-closure events during protein folding: Rationalizing the shape of Phi-value distributions
| dc.creator | Weikl, Thomas R. | |
| dc.date | 2005-02-15 | |
| dc.date.accessioned | 2026-07-07T05:58:55Z | |
| dc.date.available | 2026-07-07T05:58:55Z | |
| dc.description | In the past years, the folding kinetics of many small single-domain proteins has been characterized by mutational Phi-value analysis. In this article, a simple, essentially parameter-free model is introduced which derives folding routes from native structures by minimizing the entropic loop-closure cost during folding. The model predicts characteristic folding sequences of structural elements such as helices and beta-strand pairings. Based on few simple rules, the kinetic impact of these structural elements is estimated from the routes and compared to average experimental Phi-values for the helices and strands of 15 small, well-characterized proteins. The comparison leads on average to a correlation coefficient of 0.62 for all proteins with polarized Phi-value distributions, and 0.74 if distributions with negative average Phi-values are excluded. The diffuse Phi-value distributions of the remaining proteins are reproduced correctly. The model shows that Phi-value distributions, averaged over secondary structural elements, can often be traced back to entropic loop-closure events, but also indicates energetic preferences in the case of a few proteins governed by parallel folding processes. | |
| dc.description | 24 pages, 3 figures, 2 tables; to appear in "Proteins: Structure, Function, and Bioinformatics" | |
| dc.identifier | https://arxiv.org/abs/q-bio/0502016 | |
| dc.identifier | http://arxiv.org/abs/q-bio/0502016 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/88541 | |
| dc.subject | Biomolecules | |
| dc.subject | Soft Condensed Matter | |
| dc.title | Loop-closure events during protein folding: Rationalizing the shape of Phi-value distributions | |
| dc.type | text |