Characterization of caged compounds binding to proteins by NMR spectroscopy

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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 ligancls using different techniques Strategies to avoid non-specific binding of caged compound to certain proteins are also suggested.
Original languageUnknown
Pages (from-to)447-451
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 1 Jan 2010

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