[Conformation of the enkephalin cycloanalog Lys-Tyr-Gly-Gly-Phe-Leu-].
The spatial structure of an enkephaline cycloanalogue Lys-Tyr-Gly-Gly-Phe-Leu--has been investigated by means of energy calculations, fluorescence and CD-spectroscopy. Despite the high conformational mobility of the cycloanalogue, little resemblance exists between its and parent peptide's low-energy structures. Conformational factors for possible mechanisms of interaction between specific enkephalin receptors and cycloanalogue are discussed.
D002942:Circular Dichroism; D004743:Enkephalin, Leucine / Q000031:analogs & derivatives*; D010456:Peptides, Cyclic; D011487:Protein Conformation
D010456:Peptides, Cyclic; D004743:Enkephalin, Leucine; C047199:cyclo(lysyl-tyrosyl-glycyl-glycyl-phenylalanyl-leucyl)
Prostranstvennaia struktura molekuly tsikloanaloga énkefalina Lys-Tyr-Gly-Gly-Phe-Leu-.