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Özünde Düzensiz Proteinlerin Çoklu fosforilasyon Saptanma Nükleer Manyetik Rezonans Spektroskopisi
JoVE Journal
Biochimica
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JoVE Journal Biochimica
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
DOI:

12:47 min

December 27, 2016

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Capitoli

  • 00:05Titolo
  • 01:15Production of 15N, 13C-Tau
  • 04:18Purification of 15N, 13C-Tau
  • 07:38Acquisition of NMR Spectra
  • 10:28Results: Evaluation of the Purification Procedure of the Recombinant Protein and NMR Spectrum
  • 11:35Conclusion

Summary

Traduzione automatica

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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