[Simulation of alpha-helix and beta-hairpin formation in water-soluble proteins by the code physics method]

One of the possible ways for complete and final solution of the problem of determination of three-dimensional structure of proteins on amino acid sequence is simulation of protein three-dimensional structure formation. The use of the code physics method developed by the author has been suggested to fulfill this task. The simulation of alpha-helix and beta-hairpin formation in water-soluble proteins as a start of realization of the plan is described here. The results of the simulation were compared with the experimental data for 14 proteins of no more than 50 amino acids and therefore with little number of alpha-helices and beta-strands (to meet limits of simulation process) and with secondary structure predictions by the best to data methods of protein secondary structure prediction, PSIpred, PORTER and PROFsec. Secondary structure of the proteins, obtained as a result of the simulation of alpha-helix and beta-hairpin formation using the code physics method, corresponded completely to experimental data while the secondary structure predicted by the PSIpred, PORTER and PROFsec methods differed from these data significantly.