Akademik Veri Yönetim Sistemi
NUOVO CIMENTO DELLA SOCIETA ITALIANA DI FISICA D-CONDENSED MATTER ATOMIC MOLECULAR AND CHEMICAL PHYSICS FLUIDS PLASMAS BIOPHYSICS, cilt.19, sa.6, ss.827-833, 1997 (SCI-Expanded)
Conformation energy-minimization for the sea anemone neuropeptide Antho-RFamide (Glu(1)-Gly(2)-Arg(3)-Phe(4)-NH2) was computed by molecular mechanics (MM) using an initial investigation of staggered forms examining the linkage bonds characterized by the torsion angles phi, psi and omega and the Antho-RFamide side groups characterized by the torsion angles chi(1), chi(2), chi(3)... subsequently. The energy-map for each monopeptide of the Antho-RFamide was drawn in the range between -180 degrees and 180 degrees by the step 20 degrees. Conformation facilities for monopeptides were decided from these maps. Conformation facilities for monopeptides were examined from the best choice and the results were used in the examination of dipeptides. (Glu(1)-Gly(2)) and (Arg(3)-Phe(4)-NH2) dipeptides of the (Glu(1)-Gly(2)-Arg(3)-Phe(4)-NH2) neuropeptide were examined separately. The most convenient alternation of these was determined and used in the conformation analysis of the whole molecule.