[Structural changes in the lymph nodes after burn injury].
Explore the source record for details and available documents.
Animals↗
Biomedical subjects
L I Ismailova
Publications and source records attributed to L I Ismailova.
[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.
Amino Acid Sequence↗
[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.
Amino Acid Sequence↗
[Conformation of glycopeptides with L- and D-stereoisomers of Ala and Glu amino acids].
On the base of the semi-empirical method of conformational analysis low-energetic conformations have been found for the glycopeptides with the O-beta-N-acetyl-D-muramic acid or the O-beta-N-acetyl--D-glucosaminyl-(1-4)-N-acetyl-D-muramic acid in the glycan part and L-Ala--D-GluNH2, L-Ala--L-GluNH2, D-Ala--D-GluNH2 in the peptide part. It was shown that for either molecule preferentiability of any conformation is determined mainly by interactions between dipeptide and muramic acid residue.
Alanine↗
[Theoretical conformational analysis of cardioactive peptides. I. Tetrapeptide Phe1-Met2-Arg3-Phe4-NH2 and pentapeptide Leu1-Pro2-Leu3-Arg4- NH2].
By means of semi-empirical method, an a priori conformational analysis of a cardioactive peptides was carried out. Calculations yielded the values of all dihedral angles of the backbone and side chains of the peptides various forms as well as intra- and interresidue interaction energies.
Amino Acid Sequence↗
[Theoretical conformational analysis of cardioactive peptides. II. Nonapeptide Met1-Asn2-Tyr3-Leu4-Ala5-Phe6-Pro7-Arg8-Met9-NH 2].
Theoretical conformational analysis was carried out for the cardioactive nonapeptide Met1-Met9-NH2. Calculations yielded the values of all dihedral angles of the back bone and side chains of the nonapeptide various forms as well as intra- and interresidue interaction energies.
Amino Acid Sequence↗