Prediction of beta-turns.
A residue-coupled model is proposed to predict the beta-turns in proteins. The rates of correct prediction for the 455 beta-turn tetrapeptides and 3807 non-beta-turn tetrapeptides in the training database are 94.7 and 81.3%, respectively. The rates of correct prediction for the 110 beta-turn tetrapeptides and 30,229 non-beta-turn tetrapeptides in the testing database are 80.0 and 80.2%, respectively. Compared with the rates of correct prediction based on the residue-independent model reported previously, the quality of prediction is significantly improved by the new model, implying that the residue-coupled effect along a polypeptide chain is important for the formation of reversal turns, such as beta-turns, during the process of protein folding.
Chou
K C
KC
Pharmacia & Upjohn, Kalamazoo, Michigan, USA.
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins