Quantifying Nonnative Interactions in the Protein-Folding Free-Energy Landscape

Autor(es)

Mouro, Paulo Ricardo ; Contessoto, Vinicius de Godoi ; Chahine, Jorge ; de Oliveira, Ronaldo Junio ; Pereira Leite, Vitor Barbanti

• Tipo de documento: Artigo Científico
• Fonte: BIOPHYSICAL JOURNAL; v. 111, n. 2, p. 287-293, JUL 26 2016.
• Citações Web of Science: 5

Resumo

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)

• Processo FAPESP: 14/06862-7 - Estudos computacionais em enovelamento de proteínas e engenharia de enzimas envolvidas na geração de bioetanol
• Beneficiário: Vitor Barbanti Pereira Leite
• Modalidade de apoio: Auxílio à Pesquisa - Regular