このコンテンツを視聴するには、JoVE 購読が必要です。 サインイン又は無料トライアルを申し込む。
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
18,402 Views
•
12:47 min
•
December 27, 2016
DOI:
概要
Automatically generated
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.
Explore More Videos
Nuclear Magnetic Resonance SpectroscopyIntrinsically Disordered ProteinsTau ProteinPhosphorylationMolecular RegulationDiseaseProtein InteractionProtein StructureProtein FunctionAPtc VirusTherapyProtein InhibitorsBL21 CellsPlasmid DNALuria Bertani MediumAmpicillinM9 MediumIsotope LabelingRecombinant PlasmidOptical Density
Read Article
Cite this Article
Danis, C., Despres, C., Bessa, L. M., Malki, I., Merzougui, H., Huvent, I., Qi, H., Lippens, G., Cantrelle, F., Schneider, R., Hanoulle, X., Smet-Nocca, C., Landrieu, I. Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins. J. Vis. Exp. (118), e55001, doi:10.3791/55001 (2016).
Copy