Structural organization of rimorphin and its synthetic analogs Strukturnaia organizatsiia rimorfina i ego sinteticheskikh analogov.

Akhmedov N., Makhmudova T., Xəlilov R., Zeinalova N.

Bioorganicheskaia khimiia, vol.21, no.8, pp.587-589, 1995 (Scopus) identifier identifier

  • Publication Type: Article / Article
  • Volume: 21 Issue: 8
  • Publication Date: 1995
  • Journal Name: Bioorganicheskaia khimiia
  • Journal Indexes: Scopus
  • Page Numbers: pp.587-589
  • Open Archive Collection: Article
  • Azerbaijan State University of Economics (UNEC) Affiliated: Yes

Abstract

The spatial structure and conformations of rimorphin were investigated using theoretical conformational analysis. The spatial organization of the peptide can be described by a set of 11 low-energy conformations of the backbone. By solving the reverse conformational problem, a number of modified amino acid sequences ([Ala2], [Ala3], [MePhe9], [MeLys10], [MeVal11], and [MeVal12]-analogs of rimorphin) were determined that have spatial structures corresponding to the set of low-energy conformations and should, therefore, possess physiological activity.