Progress over the first decade of CASP experiments.
CASP has now completed a decade of monitoring the state of the art in protein structure prediction. The quality of structure models produced in the latest experiment, CASP6, has been compared with that in earlier CASPs. Significant although modest progress has again been made in the fold recognition regime, and cumulatively, progress in this area is impressive. Models of previously unknown folds again appear to have modestly improved, and several mixed alpha/beta structures have been modeled in a topologically correct manner. Progress remains hard to detect in high sequence identity comparative modeling, but server performance in this area has moved forward.
Kryshtafovych
Andriy
A
Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory Livermore, California.
Venclovas
Česlovas
Č
Institute of Biotechnology, Vilnius, Lithuania.
Fidelis
Krzysztof
K
Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory Livermore, California.
Moult
John
J
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland.
D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D003198:Computer Simulation; D003201:Computers; D030562:Databases, Protein; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D040901:Proteomics / Q000379:methods*; D015203:Reproducibility of Results; D016415:Sequence Alignment; D012984:Software