Abstract
Theoretical conformational analysis was used to study the spatial structure and conformational properties of the bovine adrenal medulla dodecapeptide BAM-12P (Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10-Pro11-Glu12). Twenty-three low-energy conformations of the BAM-12P backbone were shown to represent the spatial structure of the peptide. The inverse structural problem was solved, and synthetic analogues of BAM-12P were proposed, the spatial structures of which correspond to a set of low-energy potentially physiologically active conformations of the natural dodecapeptide.
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Translated from Bioorganicheskaya Khimiya, Vol. 31, No. 3, 2005, pp. 245–250.
Original Russian Text Copyright © 2005 by Akhmedov, Tagiev, Hasanov, Makhmudova.
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Akhmedov, N.A., Tagiev, Z.H., Hasanov, E.M. et al. Spatial Structure of BAM-12P Dodecapeptide and Its Analogues. Russ J Bioorg Chem 31, 216–220 (2005). https://doi.org/10.1007/s11171-005-0030-8
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DOI: https://doi.org/10.1007/s11171-005-0030-8