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AI InsightThe space structure of the (Glu1-Leu2-Leu3-Gly4-Gly5-Arg6-Phe7-NH2) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide (Glu1-Leu2-Leu3-Gly4) and the dipeptide (Arg6-Phe7-NH2) about the monopeptide (Gly5).
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Özet
Conformational energy-minimization of the Sea Anemone and Sea Pansy neuropeptide Pol-RFamide (Glu1-Leu2-Leu3-Gly4-Gly5-Arg6-Phe7-NH2) was carried out by molecular mechanics (MM). The linkage bonds were characterized by the torsion angles q, y and w and the side groups were characterized by the torsion angles c1, c2, c3\ldots The energy-map for each monopeptide of the Pol-RFamide I was drawn in the range of -180° to 180° with increments of 20°. Conformation facilities for monopeptides were determined from these maps. These results were used in the analysis of the dipeptide (Glu1-Leu2). Then, the (Glu1-Leu2-Leu3) tripeptide was examined using the calculated results for the dipeptide. Conformational analysis of the (Glu1-Leu2-Leu3-Gly4) tetrapeptide was performed using the low-energy values for the tripeptide. The space structure of the (Glu1-Leu2-Leu3-Gly4-Gly5-Arg6-Phe7-NH2) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide (Glu1-Leu2-Leu3-Gly4) and the dipeptide (Arg6-Phe7-NH2) about the monopeptide (Gly5).
Abstract
Conformational energy-minimization of the Sea Anemone and Sea Pansy neuropeptide Pol-RFamide (Glu1-Leu2-Leu3-Gly4-Gly5-Arg6-Phe7-NH2) was carried out by molecular mechanics (MM). The linkage bonds were characterized by the torsion angles q, y and w and the side groups were characterized by the torsion angles c1, c2, c3\ldots The energy-map for each monopeptide of the Pol-RFamide I was drawn in the range of -180° to 180° with increments of 20°. Conformation facilities for monopeptides were determined from these maps. These results were used in the analysis of the dipeptide (Glu1-Leu2). Then, the (Glu1-Leu2-Leu3) tripeptide was examined using the calculated results for the dipeptide. Conformational analysis of the (Glu1-Leu2-Leu3-Gly4) tetrapeptide was performed using the low-energy values for the tripeptide. The space structure of the (Glu1-Leu2-Leu3-Gly4-Gly5-Arg6-Phe7-NH2) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide (Glu1-Leu2-Leu3-Gly4) and the dipeptide (Arg6-Phe7-NH2) about the monopeptide (Gly5).