Studies of Inhibitor Binding to Escherichia coli Purine Nucleoside Phosphorylase Using the Transferred Nuclear Overhauser Effect and Rotating-Frame Nuclear Overhauser Enhancement

NMR studies of the adenosine analog tubercidin have been carried out in the presence of Escherichia coli purine nucleoside phosphorylase (PNP) in order to characterize the conformation of the enzyme-complexed nucleoside. Although analysis of transferred NOE data at various enzyme/inhibitor ratios in...

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Veröffentlicht in:	Biochemistry (Easton) 1994-06, Vol.33 (24), p.7547-7559
Hauptverfasser:	Perlman, Michael E, Davis, Donald G, Koszalka, George W, Tuttle, Joel V, London, Robert E
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Binding, Competitive Chemical Phenomena Chemistry, Physical Crystallization Diffusion Escherichia coli Escherichia coli - enzymology Magnetic Resonance Spectroscopy Models, Molecular Molecular Conformation Protein Conformation Purine-Nucleoside Phosphorylase - antagonists & inhibitors Purine-Nucleoside Phosphorylase - chemistry Purine-Nucleoside Phosphorylase - metabolism Temperature Tubercidin - chemistry Tubercidin - metabolism
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