Spatial structure of BAM-12P dodecapeptide and its analogues

Theoretical conformational analysis was used to study the spatial structure and conformational properties of the bovine adrenal medulla dodecapeptide BAM-12P (Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10-Pro11-Glu12). Twenty-three low-energy conformations of the BAM-12P backbone were shown to...

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Bibliographic Details
Published inBioorganicheskaia khimiia Vol. 31; no. 3; p. 245
Main Authors Akhmedov, N A, Tagiev, Z G, Gasanov, E M, Makhmudova, T A
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.05.2005
Subjects
Animals
Cattle
Computational Biology
Enkephalin, Methionine - analogs & derivatives
Enkephalin, Methionine - chemistry
Opioid Peptides - chemistry
Protein Precursors - chemistry
Protein Structure, Secondary
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Summary:Theoretical conformational analysis was used to study the spatial structure and conformational properties of the bovine adrenal medulla dodecapeptide BAM-12P (Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10-Pro11-Glu12). Twenty-three low-energy conformations of the BAM-12P backbone were shown to represent the spatial structure of the peptide. The inverse structural problem was solved, and synthetic analogues of BAM-12P were proposed, the spatial structures of which correspond to a set of low-energy potentially physiologically active conformations of the natural dodecapeptide. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2005, vol. 31, no. 3; see also http://www.maik.ru.
ISSN:0132-3423