title: 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 Clementi-Plotkin analytical model. As a consequence, the optimum frustration regime for protein folding can be predicted analytically.
authors.affiliation: Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista, São José do Rio Preto, São Paulo, Brazil.
authors.forename: Paulo Ricardo
authors.initials: PR
authors.lastname: Mouro
authors.affiliation: Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista, São José do Rio Preto, São Paulo, Brazil.
authors.forename: Vinícius
authors.initials: V
authors.lastname: de Godoi Contessoto
authors.affiliation: Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista, São José do Rio Preto, São Paulo, Brazil.
authors.forename: Jorge
authors.initials: J
authors.lastname: Chahine
authors.affiliation: Laboratório de Biofísica Teórica, Departamento de Física, Instituto de Ciências Exatas, Naturais e Educação, Universidade Federal do Triângulo Mineiro, Uberaba, Minas Gerais, Brazil.
authors.forename: Ronaldo
authors.initials: R
authors.lastname: Junio de Oliveira
authors.affiliation: Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista, São José do Rio Preto, São Paulo, Brazil. Electronic address: vleite@sjrp.unesp.br.
authors.forename: Vitor Barbanti
authors.initials: VB
authors.lastname: Pereira Leite
mesh_terms: D007700:Kinetics; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins