[Spatial structure of myelopeptides: I. Conformational analysis of MP-1, MP-2, and MP-3].
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.
Akhmetov
N A
NA
Ismailova
L I
LI
Abbasly
R M
RM
Akhmedov
N F
NF
Godzhaev
N M
NM
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D013816:Thermodynamics
D009842:Oligopeptides; C048617:myelopeptides