In-Cell Solid-State NMR as a Tool to Study Proteins in Large Complexes

Authors

  • Dr. Sina Reckel,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    Search for more papers by this author
  • Dr. Jakob J. Lopez,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    Search for more papers by this author
  • Dr. Frank Löhr,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    Search for more papers by this author
  • Prof. Dr. Clemens Glaubitz,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    Search for more papers by this author
  • Prof. Dr. Volker Dötsch

    Corresponding author
    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    • Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt (Germany)
    Search for more papers by this author

Abstract

original image

A major limitation of solution NMR is molecular tumbling, which is often too slow for detection. Here we demonstrate that solid-state NMR spectroscopy in combination with flash freezing of cells can be used to detect proteins in the cellular environment and provides information on backbone chemical shifts.

Ancillary