Human beta-endorphin. 270-MHz 1H-nuclear-magnetic-resonance study of glycyl residues in aqueous solution.
1H spectra at 270 MHz of the beta h-endorphin glycyl residues in aqueous solution are reported. The chemical shifts, coupling constants and temperature coefficients are compared with those of the glycyl residues in Met-enkephalin and in a random coil model peptide. The local conformation of Tyr-Gly-Gly-Phe-segment observed in Met-enkephalin is maintained in beta h-endorphin.
D004723:Endorphins / Q000302:isolation & purification; D004744:Enkephalin, Methionine; D005998:Glycine; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012996:Solutions; D001615:beta-Endorphin
D004723:Endorphins; D012996:Solutions; D004744:Enkephalin, Methionine; D001615:beta-Endorphin; D005998:Glycine