A secondary structure evaluation of peptides based on statistics and heuristic rules.
The study of spatial folding of peptides is a very difficult task needing time-consuming elaborations. The complexity of the problem demands tools that predict in a simple manner basic properties such as the secondary structure starting from the amino acid sequence, which contains all the information necessary for the determination fo the folding of a protein. The study of secondary structure is of considerable interest, in particular the prediction of regular structures, because these regions, like alpha-helices and beta-sheets, may form nucleation sites (M.J.E. Sternberg and J.M. Thornton, Nature 2H (1978) 15-20; B. Robson and R.H. Pain, Biochem. J. 155 (1976) 331-344). The aim of this paper is to propose a procedure for the secondary structure prediction, based on statistics (B. Robson and J. Garnier, Introduction to Proteins and Protein Engineering (Elsevier, Amsterdam, 1986); J. Garnier, D.J. Osguthorpe and B. Robson, J. Mol. Biol. 120 (1977) 97-120) and heuristic rules, also taking into account experimental data.
Rauch
G
G
Istituto di Cibernetica e Biofisica C.N.R., Dipartimento di Fisica dell'Università di Genova, Italy.
D000465:Algorithms; D000818:Animals; D002645:Chickens; D003628:Database Management Systems; D008432:Mathematical Computing; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D015203:Reproducibility of Results; D013552:Swine; D014413:Tuna; D014907:Whales
D010455:Peptides