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-ProGln) 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.

Spatial structure of myelopeptides: II. Conformational analysis of MP-4, MP-5, and MP-6

“…Therefore, we set ourselves the task of determining all the conformational possibilities of six myelopeptides with known amino acid sequences. This work continues the publication of results concerning the study of spatial structure of myelopeptides [1]. We present here the total set of low-energy conformations of myelopeptides MP-4 (Phe-Arg-Pro-Arg-Ile-MetThr-Pro), MP-5 (Val-Val-Tyr-Pro-Asp), and MP-6 (Val-Asp-Pro-Pro).…”

“…In previous work [1], we described an approach to the calculation of spatial structure of the peptides MP-1-MP-3 using the method of theoretical conformational analysis. Here, this method is applied to the study of spatial structure of the MP-4, MP-5, and MP-6 molecules.…”

“…The R form of backbone was not considered, because the Asp residue precedes Pro in the sequence and is of a high energy. Only the B form of backbone was chosen for the third Pro, because this residue precedes Pro4 in the sequence [1]. The Pro4 residue was considered in two possible forms of backbone, R and B.…”