Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation.

@article{Martinez1996ConformationalPA,
  title={Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation.},
  author={Aurora Martinez and Jan Haavik and Torgeir Flatmark and Jos{\'e} Luis Arrondo Arrondo and Arturo Muga},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 33},
  pages={
          19737-42
        }
}
The conformation and stability of recombinant tetrameric human tyrosine hydroxylase isoenzyme 1 (hTH1) was studied by infrared spectroscopy and by limited tryptic proteolysis. Its secondary structure was estimated to be 42% alpha-helix, 35% beta-extended structures (including beta-sheet), 14% beta-turns, and 10% nonstructured conformations. Addition of Fe(II) or Fe(II) plus dopamine to the apoenzyme did not significantly modify its secondary structure. However, an increased thermal stability… CONTINUE READING
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