Time-resolved fluorescence of tryptophan synthase

Time-resolved and steady-state fluorescence of the tryptophan synthase α 2 β 2 complex and of the β 2 dimer from Salmonella typhimurium were measured to characterize the conformational properties of the β subunit in the presence and in the absence of the α subunit when the catalytic species internal...

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Veröffentlicht in:	Biophysical chemistry 1996-08, Vol.61 (1), p.9-22
Hauptverfasser:	Vaccari, Silvia, Benci, Sara, Peracchi, Alessio, Mozzarelli, Andrea
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Chemical Phenomena Chemistry, Physical Frequency domain fluorescence Macromolecular Substances Protein Conformation Protein conformational states Pyridoxal 5′-phosphate and tryptophan fluorescence decays Pyridoxal 5′-phosphate-dependent enzyme Salmonella typhimurium - enzymology Serine - chemistry Spectrometry, Fluorescence - methods Time Factors Tryptophan Synthase - chemistry
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