Abstract
The spatial structure of the ACTH-(7–10) molecule, a 7–10 fragment of the adrenocorticotropic hormone, with the Phe–Arg–Trp–Gly amino-acid sequence was studied by the method of theoretical conformational analysis. The potential function of the system was chosen as the sum of nonvalent, electrostatic, and torsion interactions and the energy of hydrogen bonds. The spatial structure of the Phe–Arg–Trp–Gly molecule was calculated on the basis of low-energy conformations of the corresponding amino-acid residues. It was shown that the spatial structure of a tetrapeptide molecule can be represented by eight low-energy forms of the main chain. The low-energy conformations of the molecule, as well as the values of the dihedral angles of the main and side chains of amino-acid residues, were determined; the energy of intra- and inter-residue interactions was estimated.
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Agayeva, L.N., Abdinova, A.A., Akhmedova, S.R. et al. The Spatial Structure of the ACTH-(7–10) Molecule. BIOPHYSICS 66, 531–534 (2021). https://doi.org/10.1134/S0006350921040023
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DOI: https://doi.org/10.1134/S0006350921040023