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.
D000263:Adenylate Kinase; D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004151:Dipeptides; D006736:Horses; D006801:Humans; D008433:Mathematics; D009113:Muramidase; D011487:Protein Conformation; D011506:Proteins; D012712:Serum Globulins; D013604:T-Phages / Q000032:analysis
D004151:Dipeptides; D011506:Proteins; D012712:Serum Globulins; D000263:Adenylate Kinase; D009113:Muramidase