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- W40808844 abstract "This chapter focuses on the characterization of phosphorylated target protein by phosphorus-31 nuclear magnetic resonance (31P NMR). It describes the preparation of a sample of phosphorylated protein for analysis by 31P NMR. 31P NMR can be used to assign the type of amino acid residue the phosphate is covalently attached to, such as the β-hydroxyl of a serine or threonine residue, or the N-1 or N-3 nitrogen of the imidazole ring of a histidine. 31P NMR can provide a range of information about the nature and dynamics of the phosphorylation site that cannot be obtained by other methods. The greatest strength of the NMR method is that if two or more phosphorylation sites exist on a protein, each phosphoryl group can be individually monitored by 31P NMR. 31P NMR has several important practical advantages. It is a nondestructive spectroscopic method relying on the absorption of very low radiofrequency irradiation. Thus, the sample can be recovered intact after NMR analysis. The NMR experiment can be done under the conditions of temperature and pH that are favorable for the stability of the phosphorylated protein." @default.
- W40808844 created "2016-06-24" @default.
- W40808844 creator A5032059722 @default.
- W40808844 creator A5067477469 @default.
- W40808844 date "1984-01-01" @default.
- W40808844 modified "2023-10-16" @default.
- W40808844 title "Phosphorus-31 nuclear magnetic resonance studies of phosphorylated proteins" @default.
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- W40808844 doi "https://doi.org/10.1016/0076-6879(84)07005-1" @default.
- W40808844 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6503717" @default.
- W40808844 hasPublicationYear "1984" @default.
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