| Autor: |
Akhmedov, N. A., Agaeva, L. N., Abbasli, R. M., Ismailova, L. I. |
| Zdroj: |
Biophysics; Feb2024, Vol. 69 Issue 1, p43-50, 8p |
| Abstrakt: |
A theoretical conformational analysis was performed to study the conformational possibilities for the casoxin C molecule (Tyr1–Ile2–Pro3–Ile4–Gln5–Tyr6–Val7–Leu8–Ser9–Arg10–OH). The potential function of the system was chosen as a sum of non-valence, electrostatic, and torsion interactions, and the energy of hydrogen bonds. The low-energy conformations of the casoxin C molecule were found, the values of dihedral angles of the main and side chains of the amino acid residues that make up the molecule were determined, and the energy of intra- and interresidual interactions was estimated. It has been shown that the spatial structure of the casoxin C molecule is represented by conformations of eight shapes of the peptide backbone. The results obtained can be used to elucidate the structural and structural-functional organization of casoxin molecules. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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