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Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization

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  • Thibault Viennet
  • Aldino Viegas, Heinrich Heine University Düsseldorf, Jülich Research Centre
  • ,
  • Arne Kuepper, Max Planck Institute of Molecular Physiology
  • ,
  • Sabine Arens, Heinrich Heine University Düsseldorf, Jülich Research Centre
  • ,
  • Vladimir Gelev, Sofia University St. Kliment Ohridski
  • ,
  • Ognyan Petrov, Sofia University St. Kliment Ohridski
  • ,
  • Tom N. Grossmann, Max Planck Institute of Molecular Physiology, VU University Amsterdam
  • ,
  • Henrike Heise, Heinrich Heine University Düsseldorf, Jülich Research Centre
  • ,
  • Manuel Etzkorn, Heinrich Heine University Düsseldorf, Jülich Research Centre

Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies on non-natural protein purity and concentration to increase the desired signal over the background. We here report on the efficient and specific hyperpolarization of low amounts of a target protein in a large isotope-labeled background by combining dynamic nuclear polarization (DNP) and the selectivity of protein interactions. Using a biradical-labeled ligand, we were able to direct the hyperpolarization to the protein of interest, maintaining comparable signal enhancement with about 400-fold less radicals than conventionally used. We could selectively filter out our target protein directly from crude cell lysate obtained from only 8 mL of fully isotope-enriched cell culture. Our approach offers effective means to study proteins with atomic resolution in increasingly native concentrations and environments.

Original languageEnglish
JournalAngewandte Chemie - International Edition
Pages (from-to)10746-10750
Number of pages5
Publication statusPublished - 26 Aug 2016
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim

    Research areas

  • cell lysates, NMR spectroscopy, proteins, structural biology, structure elucidation

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