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Dergiler / 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
Sayfa
257–262
Yayın Tarihi
2022-11-05
DOI
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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 Maddede Bu Makale

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Amaç & Hipotez: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).
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Temel Bulgular & Veri:The linkage bonds were characterized by the torsion angles $Theta$, $Psi$ and $Omega$ and the side groups were characterized by the torsion angles $chi_1$, $chi_2$, $chi_3$...
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Sonuç & Katkı: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$).
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri

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$).

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Bu Makaleye Atıf Yap

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

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Kaynakça (1)

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