Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 79, Issue -, Pages 119-125Publisher
WILEY
DOI: 10.1002/prot.23160
Keywords
CASP; intramolecular contacts; residue-residue contact prediction; protein structure modeling
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Funding
- National Library of Medicine (NIH/NLM) [LM007085]
- KAUST [KUK-I1-012-43]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM100482] Funding Source: NIH RePORTER
- NATIONAL LIBRARY OF MEDICINE [P41LM007085] Funding Source: NIH RePORTER
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This 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; 79(Suppl 10): 119-125. (C) 2011 Wiley-Liss, Inc.
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