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

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

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

• Nəşrin Növü: Article / Article
• Cild: 21 Say: 8
• Nəşr tarixi: 1995
• jurnalın adı: Bioorganicheskaia khimiia
• Jurnalın baxıldığı indekslər: Scopus
• Səhifə sayı: pp.587-589
• Açıq Arxiv Kolleksiyası: Məqalə
• Adres: Bəli

Qısa məlumat

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.