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Proteins. 2011;79 Suppl 10:196-207. doi: 10.1002/prot.23182. Epub 2011 Oct 14.

CASP9 results compared to those of previous CASP experiments.

Author information

1
Genome Center, University of California-Davis, 451 Health Sciences Drive, Davis, CA 95616, USA. akryshtafovych@ucdavis.edu

Abstract

The quality of structure models submitted to CASP9 is analyzed in the context of previous CASPs. Comparison methods are similar to those used in previous articles in this series, with the addition of new methods looking at model quality in regions not covered by a single best structural template, alignment accuracy, and progress for template-free models. Progress in this CASP was again modest and statistically hard to validate. Nevertheless, there are several positive trends. There is an indication of improvement in overall model quality for the midrange of template-based modeling difficulty, methods for identifying the best model from a set generated have improved, and there are strong indications of progress in the quality of template-free models of short proteins. In addition, the new examination of a model quality in regions of model not covered by the best available template reveals better performance than had previously been apparent.

PMID:
21997643
PMCID:
PMC4180080
DOI:
10.1002/prot.23182
[Indexed for MEDLINE]
Free PMC Article

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