The study of correlated mutations in alignments of homologous proteins proved to be successful not only in the prediction of their native conformation but also in the development of a two-body effective potential between pairs of amino acids. In the present work, we extend the effective potential, introducing a many-body term based on the same theoretical framework, making use of a principle of maximum entropy. The extended potential performs better than the two-body one in predicting the energetic effect of 308 mutations in 14 proteins (including membrane proteins). The average value of the parameters of the many-body term correlates with the degree of hydrophobicity of the corresponding residues, suggesting that this term partly reflects the effect of the solvent.
|Titolo:||A many-body term improves the accuracy of effective potentials based on protein coevolutionary data|
|Settore Scientifico Disciplinare:||Settore FIS/03 - Fisica della Materia|
|Data di pubblicazione:||14-lug-2015|
|Digital Object Identifier (DOI):||10.1063/1.4926665|
|Appare nelle tipologie:||01 - Articolo su periodico|