CASP: Critical Assessment of Techniques for Protein Structure Prediction, or CASP, is a community-wide experiment performed every two years by scientists studying protein folding and modeling. The goal of CASP is to assess current knowledge and techniques used to predict protein structure, paying close attention to:
    Closeness of the experimental structure to that observed;
    Correctness of any mapping of the target sequence onto the proposed structure;
    Identification of similar structures within a protein being studied to those already known;
    Comparative models and templates derived from the studied protein;
    and Progress from earlier CASPs.

Crystallographers and NMR spectroscopists provide empirical models as "solutions" to check submitted predictions against. The results of this assesment will allow the community to evaluate the effectiveness of various methods and determine where best to focus future efforts. Three main categories of predictions exist within the competition. Tertiary structure predictions include those based on templates or comparative folding, involving homologous or analogous proteins. High-resolution modeling deals with greater degrees of backbone accuracy, allowing for the study of side-chains, loops, and active sites. Other predictions include modeling residues, identifying disorder in folds, and supposing protein function.


* UPDATE 7/14/06 *
We've matched our first submission with the recently-released solution and so far we're optimistic. This target was number 321, protein PC4016A from Desulfitobacterium hafniense.























* UPDATE 7/20/06 *
We've received the results for a second protein. This target was number 304, protein NESG Hunt 1 from Escherichia coli.