Abstract

Conformation energy-minimization for the sea anemone neuropeptide Antho-RFamide (Glu1-Gly2-Arg3-Phe4-NH2) was computed by molecular mechanics (MM) using an initial investigation of staggered forms examining the linkage bonds characterized by the torsion angles φ, ψ and ω and the Antho-R Famide side groups characterized by the torsion angles Χ1 , Χ2 , Χ3 R subsequently. The energy-map for each monopeptide of the Antho-RFamide was drawn in the range between 21807 and 180° by the step 20°. 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. (Glu1 -Gly2 ) and (Arg3-Phe4-NH2) dipeptides of the (Glu1-Gly2-Arg3-Phe4-NH2) neuropeptide were examined separately. The most convenient alternation of these was determined and used in the conformation analysis of the whole molecule.

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