English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The study of correlated mutations in alignments of homologous proteins provedto be succesful not only in the prediction of their native conformation, butalso in the developement of a two-body effective potential between pairs ofamino acids. In the present work we extend the effective potential, introducinga many--body term based on the same theoretical framework, making use of aprinciple of maximum entropy. The extended potential performs better than thetwo--body one in predicting the energetic effect of 308 mutations in 14proteins (including membrane proteins). The average value of the parameters ofthe many-body term correlates with the degree of hydrophobicity of thecorresponding residues, suggesting that this term partly reflects the effect ofthe solvent.

A many-body term improves the accuracy of effective potentials based on protein coevolutionary data