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CASP9 results compared to those of previous CASP experiments
Andriy Kryshtafovych1, Krzysztof Fidelis, John Moult
1Genome Center, University of California-Davis, 451 Health Sciences Drive, Davis, CA 95616, USA. akryshtafovych@ucdavis.edu
Proteins
|October 15, 2011
Summary
Structural modeling quality in CASP9 showed modest progress, with notable improvements in template-free models and better assessment of model quality in uncharted regions. Further validation is needed for broader trends.
Area of Science:
- Computational Biology
- Structural Bioinformatics
- Protein Modeling
Background:
- The Critical Assessment of protein Structure Prediction (CASP) experiments benchmark protein structure modeling methods.
- Previous CASP assessments have tracked progress in computational protein structure prediction.
Purpose of the Study:
- To analyze the quality of structure models submitted to CASP9.
- To evaluate progress in protein structure modeling compared to previous CASP rounds.
- To introduce and apply new methods for assessing model quality.
Main Methods:
- Analysis of CASP9 structure models using established comparison techniques.
- Application of new methods to assess model quality in regions without clear templates.
- Evaluation of alignment accuracy and progress in template-free modeling.
Main Results:
- Overall progress in CASP9 was modest and statistically challenging to validate.
- Improvements observed in mid-range template-based modeling difficulty.
- Enhanced methods for selecting the best model from generated sets.
- Significant progress indicated for template-free models of short proteins.
- Better performance identified in model regions not covered by the best template.
Conclusions:
- CASP9 demonstrated positive trends, particularly in template-free modeling and assessing model quality in challenging regions.
- While overall progress is modest, specific areas show promising advancements.
- Improved methods enhance the evaluation of protein structure models.

