Conformational analysis of Pol-RFamide II (Glu(1)-Trp(2)-Leu(3)-Lys(4)-Gly(5)-Arg(6)-Phe(7)-NH2) heptapeptide
TURKISH JOURNAL OF CHEMISTRY, cilt.26, sa.6, ss.825-831, 2002 (SCI-Expanded, Scopus, TRDizin)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 26 Sayı: 6
- Basım Tarihi: 2002
- Dergi Adı: TURKISH JOURNAL OF CHEMISTRY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, TR DİZİN (ULAKBİM)
- Sayfa Sayıları: ss.825-831
- Atatürk Üniversitesi Adresli: Evet
Özet
The geometrical structure of the sea anemone and sea pansies neuropeptide Pol-RFamide Il Glu(1)-Trp(2)-Leu(3)-Lys(4)-Gly(5)-Arg(6)-Phe(7)-NH2 was carried out by molecular mechanics (MM). The linkage bonds are characterised by the torsional angles phi, psi and w and the side groups characterised by the torsional angles x(1), x(2), x(3).... subsequently. The energy-map for each monopeptide of the Pol-RFamide H was drawn in the range of -180degrees to 180degrees with increments of 20degrees. Conformation facilities for monopeptides were decided from these maps. These results were used in the analysis of the dipeptide Glu(1)-Trp(2). Then, the Glu(1)-Trp(2)-Leu(3) tripeptide was examined by using the calculated results for dipeptide. Conformational analysis of the Glu(1)-Trp(2)-Leu(3)-Lys(4) tetrapeptide was performed using the low-energy values of the tripeptide. The geometrical structure of Glu(1)-Trp(2)-Leu(3)-Lys(4)-Gly(5)-Arg(6)-Phe(7)-NH2 neuropeptide was determined by rotating the tetrapeptide Glu(1)-Trp(2)-Leu(3)-Lys(4) and the dipeptide Arg(6)-Phe(7)-NH2 about the monopeptide Gly(5) due to the minimisation of energy.