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Russian Journal of Bioorganic Chemistry

, Volume 31, Issue 3, pp 216–220 | Cite as

Spatial Structure of BAM-12P Dodecapeptide and Its Analogues

  • N. A. Akhmedov
  • Z. H. Tagiev
  • E. M. Hasanov
  • T. A. Makhmudova
Article
  • 29 Downloads

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.

Key words

BAM-12P structure and function theoretical conformational analysis 

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Copyright information

© MAIK “Nauka/Interperiodica” 2005

Authors and Affiliations

  • N. A. Akhmedov
    • 1
  • Z. H. Tagiev
    • 2
  • E. M. Hasanov
    • 2
  • T. A. Makhmudova
    • 1
  1. 1.Baku State UniversityBakuAzerbaijan
  2. 2.Azerbaijan Medical UniversityBakuAzerbaijan

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