A proton magnetic resonance study of the conformation of methionine-enkephalin as a function of pH.
It is found that methionine-enkephalin has at least two different conformations in aqueous solution, one at low and one at high pH. From inspection of titration curves and coupling constant values, it seems reasonable to conclude that these conformations are characterized by a folding so as to bring the two ends of the molecule in close proximity. This behavior parallels that found recently in (CD3)2SO as the solvent. It follows that the Phe-Met region of the molecule constitutes a relatively rigid region, but that the chain possesses flexibility around the first Gly residue. Possible implications of this behavior with respect to the receptor site are discussed.
D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008715:Methionine; D009842:Oligopeptides; D011487:Protein Conformation
D009842:Oligopeptides; D008715:Methionine