Protein Contact Map - Contact Map Prediction

Contact Map Prediction

With the availability of high numbers of genomic sequences it becomes feasible to analyze such sequences for coevolving residues. The effectiveness of this approach results from the fact that a mutation in position i of a protein is more likely to be associated with a mutation in position j than with a back-mutation in i if both positions are functionally coupled (e.g. by taking part in an enzymatic domain, or by being adjacent in a folded protein, or even by being adjacent in an oligomer of that protein).

Several statistical methods exist to extract from a multiple sequence alignment such coupled residue pairs: observed versus expected frequencies of residue pairs (OMES); the McLachlan Based Substitution correlation (McBASC); statistical coupling analysis; Mutual Information (MI) based methods; and, most recently, direct coupling analysis (DCA)

Predicted contact maps have been used in the prediction of membrane proteins where helix-helix interactions are targeted.

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