title: Direct correlation analysis improves fold recognition.
abstract: The extraction of correlated mutations through the method of direct information (DI) provides predicted contact residue pairs that can be used to constrain the three dimensional structures of proteins. We apply this method to a large set of decoy protein folds consisting of many thousand well-constructed models, only tens of which have the correct fold. We find that DI is able to greatly improve the ranking of the true (native) fold but others still remain high scoring that would be difficult to discard due to small shifts in the core beta sheets.
authors: Division of Mathematical Biology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
authors: Michael I
authors: MI
authors: Sadowski
authors: Katarzyna
authors: K
authors: Maksimiak
authors: William R
authors: WR
authors: Taylor
mesh_terms: D019295:Computational Biology; D030562:Databases, Protein; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins