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

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 Cα structure-based model to simulate a group of proteins. We found that the free-energy barrier at the transition state (ΔF) correlates with nonnative-contact variation (ΔA), and the simulated proteins are clustered according to their fold motifs. These findings are corroborated by the Clem

SUBMITTER: Mouro PR 

PROVIDER: S-EPMC4968343 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature