
AbstractThis work presents the results of the assessment of the intramolecular residue–residue contact predictions submitted to CASP9. The methodology for the assessment does not differ from that used in previous CASPs, with two basic evaluation measures being the precision in recognizing contacts and the difference between the distribution of distances in the subset of predicted contact pairs versus all pairs of residues in the structure. The emphasis is placed on the prediction of long‐range contacts (i.e., contacts between residues separated by at least 24 residues along sequence) in target proteins that cannot be easily modeled by homology. Although there is considerable activity in the field, the current analysis reports no discernable progress since CASP8. Proteins 2011; © 2011 Wiley‐Liss, Inc.
Models, Molecular, Residue-residue contact prediction, Protein Conformation, Intramolecular contacts, Molecular, Computational Biology, Proteins, casp; intramolecular contacts; protein structure modeling; residue-residue contact prediction, Models, CASP, Protein structure modeling, Software
Models, Molecular, Residue-residue contact prediction, Protein Conformation, Intramolecular contacts, Molecular, Computational Biology, Proteins, casp; intramolecular contacts; protein structure modeling; residue-residue contact prediction, Models, CASP, Protein structure modeling, Software
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