Two-dimensional NMR studies of the porcine muscle adenylate kinase.
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.
Klaus
W
W
Max-Planck-Institute for Medical Research, Department of Biophysics, Heidelberg, FRG.
Scharf
M
M
Zimmermann
S
S
Rösch
P
P
D000263:Adenylate Kinase; D000818:Animals; D009682:Magnetic Resonance Spectroscopy; D009132:Muscles / Q000201:enzymology; D010649:Phenylalanine; D010770:Phosphotransferases; D011487:Protein Conformation; D013552:Swine; D014443:Tyrosine
D014443:Tyrosine; D010649:Phenylalanine; D010770:Phosphotransferases; D000263:Adenylate Kinase