[A conformational study of kiotorphin and its biologically active analogue].
The spatial and electronic structures of kiotorphin and its biologically active analogue [D-Arg2]-kiotorphin were studied. It was shown that [D-Arg2]-kiotorphin has a more rigid structure compared with the native molecule. The D-izomerization of arginine restricts the conformational mobility of the main chain of the molecule, which completely rules out its unfolded form. The electronic characteristics of the molecule in this case substantially change.
Akhverdieva
G A
GA
Godzhaev
N M
NM
Naviev
N S
NS
D004723:Endorphins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
D004723:Endorphins; C019448:kyotorphin