Our goal is to help advance the methods of identifying protein
structure from sequence. The Center has been organized to provide the
means of objective testing of these methods via the process of blind
prediction. The Critical Assessment of protein Structure Prediction (CASP)
experiments aim at establishing the current state of the art in
protein structure prediction, identifying what progress has been made,
and highlighting where future effort may be most productively focused.
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There have been eleven previous CASP experiments.
The twelfth experiment is planned to start in May 2016.
Description of these
experiments and the full data (targets, predictions, interactive tables with
numerical evaluation results, dynamic graphs and prediction visualization tools)
can be accessed following the links:
CASP1 (1994) |
CASP2 (1996) |
CASP3 (1998) |
CASP4 (2000) |
CASP5 (2002) |
CASP6 (2004) |
CASP7 (2006) |
CASP8 (2008) |
CASP9 (2010) |
CASP10 (2012) |
CASP11 (2014) |
Raw data for the experiments held so far are archived and stored in our
In November 2011 we have opened a new rolling CASP experiment
for all-year-round testing of ab initio modeling methods:
Details of the experiments have been published in a scientific journal
Proteins: Structure, Function and Bioinformatics.
CASP proceedings include papers describing
the structure and conduct of the experiments,
the numerical evaluation measures,
reports from the assessment teams highlighting state of the art in different prediction categories,
methods from some of the most successful prediction teams,
and progress in various aspects of the modeling.
Prediction methods are assessed on the basis of the analysis of a large
number of blind predictions of protein structure. Summary of numerical
evaluation of the methods tested in the latest CASP experiment can be found
on this web page. The main numerical measures used in evaluations are described in the
papers  ,
The latter paper also contains explanations of data handling procedures
and guidelines for navigating the data presented on this website.
Some of the best performing methods are implemented as
fully automated servers
and therefore can be used by public for protein structure modeling.
To proceed to the pages related to the latest CASP
experiments click on the logo below: