Characterization of caged compounds binding to proteins by NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Aug 27;
Authors: Bandorowicz-Pikula J, Buchet R, Cañada FJ, Clémancey M, Groves P, Jiménez-Barbero J, Lancelin JM, Marcillat O, Pikula S, Sekrecka-Belniak A, Strzelecka-Kiliszek A
Photolysable caged ligands are used to investigate protein function and activity. Here, we investigate the binding properties of caged nucleotides and their photo released products to well established but evolutionary and structurally unrelated nucleotide-binding proteins, rabbit muscle creatine kinase (RMCK) and human annexin A6 (hAnxA6), using saturation transfer difference NMR spectroscopy. We detect the binding of the caged nucleotides and discuss the general implications on interpreting data collected with photolysable caged ligands using different techniques. Strategies to avoid non-specific binding of caged compound to certain proteins are also suggested.
PMID: 20804737 [PubMed - as supplied by publisher]
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
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Authors: Hsu VL, Jia X, Kearns DR
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to...
Characterization of caged compounds binding to proteins by NMR spectroscopy.
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