CASP9 results compared to those of previous casp experiments

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. © Proteins 2011; © 2011 Wiley‐Liss, Inc.

[1]  Thomas L. Madden,et al.  Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. , 1997, Nucleic acids research.

[2]  Jaime Prilusky,et al.  Assessment of CASP8 structure predictions for template free targets , 2009, Proteins.

[3]  Krzysztof Fidelis,et al.  Progress from CASP 6 to CASP 7 , 2007 .

[4]  C Venclovas,et al.  Comparison of performance in successive CASP experiments , 2001, Proteins.

[5]  David E. Kim,et al.  Sampling bottlenecks in de novo protein structure prediction. , 2009, Journal of molecular biology.

[6]  John Moult,et al.  A decade of CASP: progress, bottlenecks and prognosis in protein structure prediction. , 2005, Current opinion in structural biology.

[7]  Krzysztof Fidelis,et al.  CASP: A Driving Force in Protein Structure Modeling , 2010 .

[8]  Matthew P Jacobson,et al.  Assessment of protein structure refinement in CASP9 , 2011, Proteins.

[9]  Torsten Schwede,et al.  Assessment of template based protein structure predictions in CASP9 , 2011, Proteins.

[10]  Michael J. E. Sternberg,et al.  Sequencing delivers diminishing returns for homology detection: implications for mapping the protein universe , 2010, Bioinform..

[11]  A. Godzik,et al.  A general method for the prediction of the three dimensional structure and folding pathway of globular proteins: Application to designed helical proteins , 1993 .

[12]  Johannes Söding,et al.  Protein homology detection by HMM?CHMM comparison , 2005, Bioinform..

[13]  Krzysztof Fidelis,et al.  CASP8 results in context of previous experiments , 2009, Proteins.

[14]  N. Grishin,et al.  CASP9 target classification , 2011, Proteins.

[15]  Ceslovas Venclovas,et al.  Assessment of progress over the CASP experiments , 2003, Proteins.

[16]  Krzysztof Fidelis,et al.  Progress from CASP6 to CASP7 , 2007, Proteins.

[17]  Yang Zhang Progress and challenges in protein structure prediction. , 2008, Current opinion in structural biology.

[18]  Ceslovas Venclovas,et al.  Progress over the first decade of CASP experiments , 2005, Proteins.

[19]  Adam Zemla,et al.  LGA: a method for finding 3D similarities in protein structures , 2003, Nucleic Acids Res..

[20]  Iakes Ezkurdia,et al.  Target domain definition and classification in CASP8 , 2009, Proteins.