Assessment of disorder predictions in CASP6.
Natively disordered proteins or protein segments are those without stable secondary or tertiary structure in the absence of binding partners. Such disordered regions often are important functional sites in many biological processes, especially those involved in transcription, translation, and cell signaling. The prediction of such regions is therefore of great importance in focusing experimental efforts on regions of proteins that may be critical for function. In CASP6, held in 2004, twenty research groups participated in the prediction of disordered regions. Both binary predictions (ordered or disordered) and assigned scores for disorder were assessed. Several groups performed quite well in predicting regions of disorder in the X-ray and NMR structures available to the assessors. The best of these groups performed better than the best groups in CASP5, held in 2002.
Jin
Yumi
Y
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia Pennsylvania.
Dunbrack
Roland L
RL
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia Pennsylvania.
D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D003198:Computer Simulation; D003201:Computers; D030562:Databases, Protein; D006801:Humans; 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