TY - JOUR
T1 - Evaluation of residue-residue contact predictions in CASP9
AU - Monastyrskyy, Bohdan
AU - Fidelis, Krzysztof
AU - Tramontano, Anna
AU - Kryshtafovych, Andriy
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: Grant sponsor: National Library of Medicine (NIH/NLM); Grant number: LM007085; Grant sponsor: KAUST Award; Grant number: KUK-I1-012-43.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.
PY - 2011/9/17
Y1 - 2011/9/17
N2 - 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.
AB - 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.
UR - http://hdl.handle.net/10754/598253
UR - http://doi.wiley.com/10.1002/prot.23160
UR - http://www.scopus.com/inward/record.url?scp=80855132587&partnerID=8YFLogxK
U2 - 10.1002/prot.23160
DO - 10.1002/prot.23160
M3 - Article
C2 - 21928322
SN - 0887-3585
VL - 79
SP - 119
EP - 125
JO - Proteins: Structure, Function, and Bioinformatics
JF - Proteins: Structure, Function, and Bioinformatics
IS - S10
ER -