title: Two-dimensional NMR studies of the porcine muscle adenylate kinase.
abstract: Porcine adenylate kinase was subjected to one- and two-dimensional proton NMR studies in order to identify amino acid spin systems and obtain sequence-specific resonance assignments. With a combination of results from a map of side-chain distances resulting from the refined X-ray crystallographic data and nuclear Overhauser effect spectroscopy (NOESY), assignments are suggested for all the aromatic spin systems.
authors.affiliation: Max-Planck-Institute for Medical Research, Department of Biophysics, Heidelberg, FRG.
authors.forename: W
authors.initials: W
authors.lastname: Klaus
authors.forename: M
authors.initials: M
authors.lastname: Scharf
authors.forename: S
authors.initials: S
authors.lastname: Zimmermann
authors.forename: P
authors.initials: P
authors.lastname: Rösch
mesh_terms: D000263:Adenylate Kinase; D000818:Animals; D009682:Magnetic Resonance Spectroscopy; D009132:Muscles / Q000201:enzymology; D010649:Phenylalanine; D010770:Phosphotransferases; D011487:Protein Conformation; D013552:Swine; D014443:Tyrosine
chemical_list: D014443:Tyrosine; D010649:Phenylalanine; D010770:Phosphotransferases; D000263:Adenylate Kinase