Genome Center, University of California-Davis, 451 Health Sciences Drive, Davis, CA 95616, USA.
Proteins. 2011;79 Suppl 10(0 10):196-207. doi: 10.1002/prot.23182. Epub 2011 Oct 14.
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.
在以前的 CASP 中分析了提交给 CASP9 的结构模型的质量。比较方法与本系列以前的文章中使用的方法相似,新增了一些方法,用于研究单个最佳结构模板未涵盖的区域的模型质量、对准精度和无模板模型的进展。该 CASP 的进展再次较为适度,且在统计学上难以验证。尽管如此,还是有一些积极的趋势。对于基于模板建模难度的中等范围,整体模型质量有改善的迹象,从一组生成的模型中识别最佳模型的方法有所改进,并且短蛋白质无模板模型的质量也有明显的进步迹象。此外,对最佳可用模板未覆盖的模型区域的模型质量进行的新检查显示出比以前更为出色的性能。