title: A photochemically induced dynamic nuclear polarization study of pancreatic phospholipase A2. NMR assignment of some aromatic residues.
abstract: Application of the photochemically induced dynamic nuclear polarization technique to porcine pancreatic phospholipase A2 and its precursor resulted in the observation of nuclear spin polarization for the single tryptophan and 2 tyrosine residues. Using selectively nitrated enzymes, the tyrosine resonances could be assigned to residues 69 and 123. Both tryptophan-3 and tyrosine-69 are of particular interest because they are part of the lipid binding site.
mesh_terms: D001665:Binding Sites; D009682:Magnetic Resonance Spectroscopy; D010179:Pancreas / Q000201:enzymology*; D010740:Phospholipases; D010777:Photochemistry; D014364:Tryptophan; D014443:Tyrosine
chemical_list: D014443:Tyrosine; D014364:Tryptophan; D010740:Phospholipases