title: A many-body term improves the accuracy of effective potentials based on protein coevolutionary data.
abstract: 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.
authors.affiliation: Department of Physics, Università degli Studi di Milano, via Celoria 16, 20133 Milano, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Contini
authors.affiliation: Department of Physics, Università degli Studi di Milano, and INFN, via Celoria 16, 20133 Milano, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Tiana
mesh_terms: D019277:Entropy; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D009154:Mutation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*
chemical_list: D011506:Proteins