| Full text | |
| Author(s): |
Mouro, Paulo Ricardo
;
Contessoto, Vinicius de Godoi
;
Chahine, Jorge
;
de Oliveira, Ronaldo Junio
;
Pereira Leite, Vitor Barbanti
Total Authors: 5
|
| Document type: | Journal article |
| Source: | BIOPHYSICAL JOURNAL; v. 111, n. 2, p. 287-293, JUL 26 2016. |
| Web of Science Citations: | 5 |
| Abstract | |
Protein folding is a central problem in biological physics. Energetic roughness is an important aspect that controls protein-folding stability and kinetics. The roughness is associated with conflicting interactions in the protein and is also known as frustration. Recent studies indicate that an addition of a small amount of energetic frustration may enhance folding speed for certain proteins. In this study, we have investigated the conditions under which frustration increases the folding rate. We used a C-alpha structure-based model to simulate a group of proteins. We found that the free-energy barrier at the transition state (Delta F) correlates with nonnative-contact variation (Delta A), and the simulated proteins are clustered according to their fold motifs. These findings are corroborated by the Clementi-Plotkin analytical model. As a consequence, the optimum frustration regime for protein folding can be predicted analytically. (AU) | |
| FAPESP's process: | 14/06862-7 - Computational studies in protein folding and enzymes engineering involved in bioethanol production |
| Grantee: | Vitor Barbanti Pereira Leite |
| Support Opportunities: | Regular Research Grants |