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تسجيل مستخدم جديدA many-body term improves the accuracy of effective potentials based on protein coevolutionary data
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The study of correlated mutations in alignments of homologous proteins proved to be succesful not only in the prediction of their native conformation, but also in the developement 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.
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