2015/06/08 by Alessandro Contini, Guido Tiana, Contini, A. +1 · 1 citation
Biochemistry, Genetics and Molecular Biology · #Biomolecules (q-bio.BM) #Evolution and Genetic Dynamics #FOS: Biological sciences #Protein Structure and Dynamics #RNA and protein synthesis mechanisms
paper · pdf · doi:10.48550/arxiv.1506.02379
openalex publication_date 2015/06/08 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28
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.