[Tertiary structure of myelopeptides. II. Conformational analysis of Phe-Arg-Pro-Arg-Ile-Met-Thr-Pro, Val-Val-Tyr-Pro-Asp, and Val-Asp-Pro-Pro].
Theoretical conformational analysis was used to study the spatial structure and conformational properties of myelopeptides, bone marrow peptide mediators. The low-energy conformations of myelopeptides MP-4 (Phe-Arg-Pro-Arg-Ile-Met-Thr-Pro), MP-5 (Val-Val-Tyr-Pro-Asp), and MP-6 (Val-Asp-Pro-Pro) were found; the values of dihedral angles of backbone and side chains of the amino acid residues were determined; and the energies of intra- and interresidual interactions were estimated.
Ismailova
L I
LI
Akhmetov
N A
NA
Abbasly
R M
RM
Godzhaev
N M
NM
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D013816:Thermodynamics
D009842:Oligopeptides; C502954:phenylalanyl-arginyl-prolyl-arginyl-isoleucyl-methionyl-threonyl-proline; C502956:valyl-aspartyl-prolyl-proline; C502955:valyl-valyl-tyrosyl-prolyl-aspartic acid; C048617:myelopeptides