Dergiler / Turkish Journal of Chemistry / 2002 / Cilt: 26 - Sayı: 6
Conformational Analysis of Pol-Rfamide II (Glu}1-Trp2-Leu3-Lys4-Gly5-Arg6-Phe7-NH2) Heptapeptide
- Sayfa
- 825–832
- DOI
- —
Özet
The geometrical structure of the sea anemone and sea pansies neuropeptide Pol-RFamide II Glu1-Trp2-Leu3-Lys4-Gly5-Arg6-Phe7-NH2 was carried out by molecular mechanics (MM). The linkage bonds are characterised by the torsional angles f, y and w and the side groups characterised by the torsional angles c1, c2, c3,... subsequently. The energy-map for each monopeptide of the Pol-RFamide II was drawn in the range of -180° to 180° with increments of 20°. Conformation facilities for monopeptides were decided from these maps. These results were used in the analysis of the dipeptide Glu1-Trp2. Then, the Glu1-Trp2-Leu3 tripeptide was examined by using the calculated results for dipeptide. Conformational analysis of the Glu1-Trp2-Leu3-Lys4 tetrapeptide was performed using the low-energy values of the tripeptide. The geometrical structure of Glu1-Trp2-Leu3-Lys4-Gly5-Arg6-Phe7-NH2 neuropeptide was determined by rotating the tetrapeptide Glu1-Trp2-Leu3-Lys4 and the dipeptide Arg6-Phe7-NH2 about the monopeptide Gly5 due to the minimisation of energy.
Abstract
The geometrical structure of the sea anemone and sea pansies neuropeptide Pol-RFamide II Glu1-Trp2-Leu3-Lys4-Gly5-Arg6-Phe7-NH2 was carried out by molecular mechanics (MM). The linkage bonds are characterised by the torsional angles f, y and w and the side groups characterised by the torsional angles c1, c2, c3,... subsequently. The energy-map for each monopeptide of the Pol-RFamide II was drawn in the range of -180° to 180° with increments of 20°. Conformation facilities for monopeptides were decided from these maps. These results were used in the analysis of the dipeptide Glu1-Trp2. Then, the Glu1-Trp2-Leu3 tripeptide was examined by using the calculated results for dipeptide. Conformational analysis of the Glu1-Trp2-Leu3-Lys4 tetrapeptide was performed using the low-energy values of the tripeptide. The geometrical structure of Glu1-Trp2-Leu3-Lys4-Gly5-Arg6-Phe7-NH2 neuropeptide was determined by rotating the tetrapeptide Glu1-Trp2-Leu3-Lys4 and the dipeptide Arg6-Phe7-NH2 about the monopeptide Gly5 due to the minimisation of energy.