[Structural organization of rimorphin and its synthetic analogs].
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.
Akhmedov
N A
NA
Makhmudova
T A
TA
Khalilov
R I
RI
Zeĭnalova
N M
NM
D000595:Amino Acid Sequence; D004399:Dynorphins / Q000737:chemistry* / Q000502:physiology; D004723:Endorphins / Q000737:chemistry* / Q000502:physiology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D004723:Endorphins; D004399:Dynorphins; C036200:rimorphin
Strukturnaia organizatsiia rimorfina i ego sinteticheskikh analogov.