title: [Spatial structure of myelopeptides: I. Conformational analysis of MP-1, MP-2, and MP-3].
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 constituting these peptides were determined, and the energies of intra- and interresidual interactions were estimated.
authors.forename: N A
authors.initials: NA
authors.lastname: Akhmetov
authors.forename: L I
authors.initials: LI
authors.lastname: Ismailova
authors.forename: R M
authors.initials: RM
authors.lastname: Abbasly
authors.forename: N F
authors.initials: NF
authors.lastname: Akhmedov
authors.forename: N M
authors.initials: NM
authors.lastname: Godzhaev
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D009842:Oligopeptides; C048617:myelopeptides