Abstract
Theoretical conformational analysis was used to study the spatial structure and conformational properties of myelopeptides, bone-marrow peptide mediators. The low-energy conformations of three hexapeptides MP-1 (Phe-Leu-Gly-Phe-Pro-Thr), MP-2 (Leu-Val-Val-Tyr-Pro-Trp), and MP-3 (Leu-Val-Cys-Tyr-Pro-Gln) were found, the values of dihedral angles of the backbone and side chains of the amino acid residues con-stituting these peptides were determined, and the energies of intra- and interresidual interactions were estimated.
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Translated from Bioorganicheskaya Khimiya, Vol. 31, No. 1, 2005, pp. 31–38.
Original Russian Text Copyright © 2005 by Akhmedov, Ismailova, Abbasli, Akhmedov, Godjaev.
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Akhmedov, N.A., Ismailova, L.I., Abbasli, R.M. et al. Spatial structure of myelopeptides: I. conformational analysis of MP-1, MP-2, and MP-3. Russ J Bioorg Chem 31, 27–33 (2005). https://doi.org/10.1007/s11171-005-0003-y
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DOI: https://doi.org/10.1007/s11171-005-0003-y