N M Godzhaev

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The spatial structure of the neurokinin A molecule was studied by the method of theoretical conformational analysis. On the basis of fragmental analysis, stable structures of the neurokinin A molecule under polar conditions were determined. The structures can be described by four families of low-energy conformations having a relatively labile tripeptide at(More)
The spatial structure of cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule has been investigated using a theoretical conformational analysis. The low-energy conformations of the molecule were found, the values of the backbone and side T-T chain dihedral angles of amino acid residues constituting the peptide were determined, and the energies of(More)
Conformational energy calculations were carried out for beta-endorphin. Its spatial structure can be described by nine low-energy conformations. The calculations yielded the values of all dihedral angles of the backbone and side chains of these forms as well as intra- and inter-residue interaction energies.
Theoretical small-angle diffuse scattering curves from muscle thin filament models have been calculated. The curves reveal a maximum at 115' scattering angle. It has been shown that the maximum is due to the pitch of F-actin helix. Theoretical curves are in good agreement with the earlier obtained curves of small-angle diffuse scattering from F-actin dilute(More)
The spatial and electronic structures of kiotorphin and its biologically active analogue [D-Arg2]-kiotorphin were studied. It was shown that [D-Arg2]-kiotorphin has a more rigid structure compared with the native molecule. The D-izomerization of arginine restricts the conformational mobility of the main chain of the molecule, which completely rules out its(More)
Conformational energy calculations were carried out for neuropeptides alpha-, gamma- and delta-endorphins, which are 1-16, 1-17 and 1-19 fragments respectively, of beta-endorphin. The proposed computational scheme yielded all possible low-energy conformational sets for these hormones. Specific features of spatial organization of each compound and(More)
The spatial structures of human immunoglobulin E pentapeptide Asp-Ser-Asp-Pro-Arg and some of its related peptides were investigated by the method of theoretical conformational analysis. These synthetic peptides have the capacity to inhibit the binding of immunoglobulin E to the mast cells of the skin. The results of the calculations and the data on(More)