CASP8 results in context of previous experiments.
The quality of structure models submitted to CASP8 is analyzed in the context of previous CASPs. To compare models from the latest experiment with their predecessors, we use the approaches consistent with the previous articles in this series. Using the basic evaluation measures accepted in CASP, there were no noticeable advances in the quality of the methods in any of the target difficulty categories. At the same time, there were three positive developments: (1) for set of the best models on each target, CASP8 registered the highest number of cases from all CASPs where alignment accuracy exceeded the maximum possible from the best template; (2) modeling accuracy of regions not present in the best template has improved; and (3) the loss in modeling quality from selection of nonoptimal models as the best ones submitted on the target has decreased.
Kryshtafovych
Andriy
A
Genome Center, University of California, Davis, California 95616, USA. akryshtafovych@ucdavis.edu
Fidelis
Krzysztof
K
Moult
John
J
D019295:Computational Biology / Q000379:methods*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*
D011506:Proteins