The investigation of [(4'-amino)-PHE]4-enkephalin conformation in water by the spectrofluorimetric procedure.
The intramolecular distance between the aromatic rings of tyrosine and 4'-aminophenylalanine in Tyr-Gly-Gly-(p-NH2)Phe-Leu was determined spectrofluorimetrically. On the basis of the data obtained, conformation of the analogue of Leu-enkephalin (an endogenous pentapeptide with morphine-like activity) was established. From tyrosine fluorescence quenching and relative enhancement of 4'-aminophenylalanine fluorescence, the efficiency of intramolecular energy transfer between tyrosine and 4'-aminophenylalanine was determined and the average distance between fluorophores was calculated to be about 1 nm.
D004723:Endorphins / Q000032:analysis*; D004743:Enkephalin, Leucine / Q000031:analogs & derivatives*; D004745:Enkephalins / Q000032:analysis*; D008968:Molecular Conformation; D010649:Phenylalanine / Q000032:analysis; D013050:Spectrometry, Fluorescence; D014443:Tyrosine / Q000032:analysis; D014867:Water / Q000032:analysis
D004723:Endorphins; D004745:Enkephalins; D014867:Water; D014443:Tyrosine; D010649:Phenylalanine; D004743:Enkephalin, Leucine; C029940:enkephalin-Leu, NH2(3)-