Email this article Spatial Structure of the Casoxin C Molecule
- Authors: Akhmedov N.А1, Agaeva L.N1, Abbasli R.M1, Ismailova L.I1
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Affiliations:
- Institute for Physical Problems, Baku State University
- Issue: Vol 69, No 1 (2024)
- Pages: 53-61
- Section: Molecular biophysics
- URL: https://journals.rcsi.science/0006-3029/article/view/257124
- DOI: https://doi.org/10.31857/S0006302924010051
- EDN: https://elibrary.ru/RGZNER
- ID: 257124
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Abstract
A theoretical conformational analysis was performed to study the conformational possibilities for thecasoxin C molecule (Tyr1-Ile2-Pro3-Ile4-Gln5-Tyr6-Val7-Leu8-Ser9-Arg10-OH). The potential functionof the system is 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 dihedralangles 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 skeleton. Theresults obtained can be used to elucidate the structural and structural-functional organization of casoxin molecules.
Keywords
About the authors
N. А Akhmedov
Institute for Physical Problems, Baku State University
Email: Namiq.49@bk.ru
ul. Z. Khalilova 23, Baku, AZ-1148, Azerbaijan
L. N Agaeva
Institute for Physical Problems, Baku State Universityul. Z. Khalilova 23, Baku, AZ-1148, Azerbaijan
R. M Abbasli
Institute for Physical Problems, Baku State Universityul. Z. Khalilova 23, Baku, AZ-1148, Azerbaijan
L. I Ismailova
Institute for Physical Problems, Baku State Universityul. Z. Khalilova 23, Baku, AZ-1148, Azerbaijan
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