SavedAdd your journal

Journals / Turkish Journal of Chemistry / 1999 / Cilt: 23 - Sayı: 3

Conformational analysis of linear peptide ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7NH_2$)

L. DEMİR
Y. ŞAHİN
A. KARABULUT
G. BUDAK
N. SEFTEROĞLU
Pages
257–262
Publication Date
2022-11-05
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

The space structure of the ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7-NH_2$) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide ($Glu^1-Leu^2-Leu^3-Gly^4) and the dipeptide ($Arg^6-Phe^7-NH_2$) about the monopeptide ($Gly^5$).

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Conformational energy-minimization of the Sea Anemone and Sea Pansy neuropeptide Pol-RFamide ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7-NH_2$) was carried out by molecular mechanics (MM).
📊
Key Findings & Data:The linkage bonds were characterized by the torsion angles $Theta$, $Psi$ and $Omega$ and the side groups were characterized by the torsion angles $chi_1$, $chi_2$, $chi_3$...
💡
Conclusion & Impact:The space structure of the ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7-NH_2$) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide ($Glu^1-Leu^2-Leu^3-Gly^4) and the dipeptide ($Arg^6-Phe^7-NH_2$) about the monopeptide ($Gly^5$).
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

Conformational energy-minimization of the Sea Anemone and Sea Pansy neuropeptide Pol-RFamide ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7-NH_2$) was carried out by molecular mechanics (MM). The linkage bonds were characterized by the torsion angles $Theta$, $Psi$ and $Omega$ and the side groups were characterized by the torsion angles $chi_1$, $chi_2$, $chi_3$... 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 ($Glu^1-Leu^2$). Then, the ($Glu^1-Leu^2-Leu^3$) tripeptide was examined using the calculated results for the dipeptide. Conformational analysis of the ($Glu^1-Leu^2-Leu^3-Gly^4$) tetrapeptide was performed using the low-energy values for the tripeptide. The space structure of the ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7-NH_2$) neuropeptide was found as a result of minimization of energies by rotating the tetrapeptide ($Glu^1-Leu^2-Leu^3-Gly^4) and the dipeptide ($Arg^6-Phe^7-NH_2$) about the monopeptide ($Gly^5$).

🔖

Cite This Article

DEMİR, L., ŞAHİN, Y., KARABULUT, A., BUDAK, G., SEFTEROĞLU, N. (2022). Conformational analysis of linear peptide ($Glu^1-Leu^2-Leu^3-Gly^4-Gly^5-Arg^6-Phe^7NH_2$). Turkish Journal of Chemistry, Cilt: 23 - Sayı: 3, 257–262. https://ajindex.com/articles/602469

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (1)

  1. Grimmelikhuijzen, C. J. P., Rinehart, K. L. and Spencer, A. N., Biochem. Biophys. Res. Commun., 183, 375(1992). 2. Radom, L., Lathan, W. A., Hehre, W. J., Pople, J. A., J. Am. Chem. Soc., 95, 693 (1973). 3. B ̈ocker, J., Brickman, J. and Bopp P., J. Phys. Chem., 98, 712 (1994). 4. Boyd, R. H., Gee, R. H., Han, J. and Jin, Y., J. Chem. Phys., 101 (1), 788 (1994). 5. Meyer, C., Perez, S., Herve du Penhoat C., J. Am. Chem. Soc., 115, 10300 (1993). 6. Orti, E., Viruela, P. M., Marin, J. S. and Tomas. F., J. Phys. Chem., 99, 4955 (1995). 7. Quirante, J. J., J. Anal. Appl. Pyrolysis., 31, 169 (1995). 8. K ̈over, K. E., Jiao, D., Fang, S. and Hruby, V. J., J. Org. Chem., 59, 991 (1994). 9. Tobiason, F. L., Fronczek, F. R., Steynberg., J. P., Steynberg, E. C. and Hemingway, R. W., Tetrahedron., 27,5927 (1993). 10. Perzel, A., McAllister, M. A., Csaszar, P. and Csizmadia, I. G., J. Am.115, 4849 (1993). 11. Waterhouse, A. L., Horvath, K. and Liu, J., carbohydr. Res., 235, 1 (1992). 12. Oka, M., Baba, Y. Kagemoto, A. and Nakajima, A., Polym. J., 21, 1011 (1989). 13. Subramanian, E. and Sahayamary, J. J., Int. J. Peptide Protein Res., 41, 319 (1993). 14. Momany, F. A., McGuire, R. F., Bugess, A. W. and Scheraga, H. A., J. Phys. Chem., 79, 2361 (1975). 15. Akhmedov, N. A., Akhveerdieva, G. A., Godjaev, N. M. and Popv, E. M., Int. J. Peptide Protein Res., 27, 112(1986). 16. Demir, L., Sefteroglu, N., Budak, G., Karabulut, A. and Sahin, Y., Il Nuovo Cimento, 19 D, 827 (1997)