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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
JoVE Journal
Biochemistry
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JoVE Journal Biochemistry
Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

DOI:
10.3791/58537-v

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10:28 min

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November 02, 2018

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, , ,
1Department of Biochemistry,University of Alberta

Chapters

  • 00:04Title
  • 00:24NMR Experimental Setup
  • 04:25NMR Data Processing
  • 05:47NMR Data Analysis
  • 08:13Results: Vimentin 99-249 (VimRod) Binds Wildtype Envoplakin Plakin Repeat Domain (E-PRD) but not Mutant R1914E E-PRD
  • 09:54Conclusion

Summary

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Here, we present a protocol for the production and purification of proteins that are labeled with stable isotopes, and subsequent characterization of protein-protein interactions using Nuclear Magnetic Resonance (NMR) spectroscopy and MicroScale Thermophoresis (MST) experiments.

Tags

Keywords: Protein InteractionNMR SpectroscopyMicroscale ThermophoresisMSTAtomic-level InteractionProtein BindingSmall MoleculeLarge MoleculeProton NMRSOFAST HMBCMagnetic Field ShimmingReceiver Gain AdjustmentAutomatic TuningPhase CorrectionBaseline Correction

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