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JoVE Journal Biochemistry
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
 

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Article DOI: 10.3791/55001-v • 12:47 min • December 27th, 2016
December 27th, 2016 •
*1,2, *1, 1, 1, 1, 1, 1, 1, 1, 1, 1, 1, 1
1UMR8576, CNRS, Lille University, 2UMR-S1172, INSERM CNRS, Lille University
* These authors contributed equally

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We describe here a method to identify multiple phosphorylations of an intrinsically disordered protein by Nuclear Magnetic Resonance Spectroscopy (NMR), using Tau protein as a case study. Recombinant Tau is isotopically enriched and modified in vitro by a kinase prior to data acquisition and analysis.

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Nuclear Magnetic Resonance Spectroscopy Identification Multiple Phosphorylations Intrinsically Disordered Proteins Tau Protein Molecular Regulation Disease Protein Interaction Site-specific Phosphorylation Structural Changes Functional Changes Insight Into Function Therapy Protein-protein Interaction Inhibitors Clement Danis Clement Despres Luiza Bessa Hamida Merzougui PhD Students
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