Prediction of the secondary structure of globular proteins by their amino acid sequence

Prediction algorithms for protein secondary structures by amino acid sequence based on a statistical analysis of 46 proteins have been devised. The ith residual chain is assumed to be in one of four states: alpha-helix, beta-sheet, beta-turn or random coil conformation. It is shown that algorithm enables to predict properly 85.9% of the residual states in alpha-helical conformation, 72.4% in beta-sheet conformation, and 70.7% in beta-turn conformation. A comparison has been made with other prediction methods of the protein secondary structure, and it is pointed out that the algorithms proposed are the most effective ones.