title: [Spatial structure of BAM-12P dodecapeptide and its analogues].
abstract: 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.
authors: N A
authors: NA
authors: Akhmedov
authors: Z G
authors: ZG
authors: Tagiev
authors: E M
authors: EM
authors: Gasanov
authors: T A
authors: TA
authors: Makhmudova
mesh_terms: D000818:Animals; D002417:Cattle; D019295:Computational Biology; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000737:chemistry*; D018847:Opioid Peptides / Q000737:chemistry*; D011498:Protein Precursors / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D018847:Opioid Peptides; D011498:Protein Precursors; D004744:Enkephalin, Methionine; C026771:BAM 12P