Artículo
Inferring repeat-protein energetics from evolutionary information
Fecha de publicación:
06/2017
Editorial:
Public Library of Science
Revista:
Plos Computational Biology
ISSN:
1553-734X
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Natural protein sequences contain a record of their history. A common constraint in a given protein family is the ability to fold to specific structures, and it has been shown possible to infer the main native ensemble by analyzing covariations in extant sequences. Still, many natural proteins that fold into the same structural topology show different stabilization energies, and these are often related to their physiological behavior. We propose a description for the energetic variation given by sequence modifications in repeat proteins, systems for which the overall problem is simplified by their inherent symmetry. We explicitly account for single amino acid and pair-wise interactions and treat higher order correlations with a single term. We show that the resulting evolutionary field can be interpreted with structural detail. We trace the variations in the energetic scores of natural proteins and relate them to their experimental characterization. The resulting energetic evolutionary field allows the prediction of the folding free energy change for several mutants, and can be used to generate synthetic sequences that are statistically indistinguishable from the natural counterparts.
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(IQUIBICEN)
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES
Citación
Espada, Rocío; Parra, Rodrigo Gonzalo; Mora, Thierry; Walczak, Aleksandra M.; Ferreiro, Diego; Inferring repeat-protein energetics from evolutionary information; Public Library of Science; Plos Computational Biology; 13; 6; 6-2017; 1-16
Compartir
Altmétricas