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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

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

Published on: December 27, 2016

メチル-TROSY NMRを用いた670 kDaのプロテアソーム核粒子における活性部位イオン化均衡の測定

Algirdas Velyvis1, Lewis E Kay

  • 1Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada M5S 1A8. avelyvis@pound.med.utoronto.ca

Journal of the American Chemical Society
|June 27, 2013
PubMed
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The Proteasome Structure

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¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

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Proton (¹H) NMR: Chemical Shift

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NMR Spectroscopy Of Amines

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Mass Spectrometry: Isotope Effect

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