Solid-state NMR Spectroscopy and Dynamic Nuclear Polarization

Royal Society of Chemistry eBooks, pp. 43–76

Abstract

Solid-state nuclear magnetic resonance (NMR) has become an important player in integrated structural biology approaches, particularly benefiting from the high sensitivity of NMR observables for small structural changes or ligand binding, the simple sample preparation based on sedimentation and the absence of any molecular-weight-dependent resonance broadening. The development of ultra-high magnetic-field strengths (>28 T) and fast magic-angle spinning techniques (>100 kHz) allows the study of, for instance, large proteins and their complexes, supramolecular assemblies or membrane proteins embedded in lipids requiring only sub-milligram amounts of protein sample. The basic principles of biomolecular solid-state NMR, sample preparation schemes and signal enhancement tools using dynamic nuclear polarization are discussed herein. Some recent examples for solid-state NMR embedded in the toolbox of integrated structural biology are presented in this chapter, focusing on employing solid-state NMR in concert with cryo-electron microscopy, X-ray diffraction, solution-state NMR, electron paramagnetic resonance and molecular dynamics simulations. Information accessible from solid-state NMR, such as protein dynamics, protein–ligand interactions, secondary-structure information and distance restraints is summarized and the strengths of solid-state NMR in protein structure determination are highlighted.

Authors 4

1. Nicole Schröder Aachen aInstitute of Technical and Macromolecular Chemistry

   RWTH Aachen University

   Affiliation as printed

   aInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Worringer Weg 2, 52074 Aachen, Germany

2. Ettore Bartalucci Aachen aInstitute of Technical and Macromolecular Chemistry

   Max Planck Institute for Chemical Energy Conversion · RWTH Aachen University

   Affiliation as printed

   aInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Worringer Weg 2, 52074 Aachen, Germany

   bMax Planck Institute for Chemical Energy Conversion, Stiftstr. 34-36, 45470 Mülheim/Ruhr, Germany

3. B. Uluca Yazgi

   Max Planck Institute for Chemical Energy Conversion

   Affiliation as printed

   bMax Planck Institute for Chemical Energy Conversion, Stiftstr. 34-36, 45470 Mülheim/Ruhr, Germany

4. Thomas Wiegand Aachen aInstitute of Technical and Macromolecular Chemistry

   Max Planck Institute for Chemical Energy Conversion · RWTH Aachen University

   Affiliation as printed

   aInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Worringer Weg 2, 52074 Aachen, Germany

   bMax Planck Institute for Chemical Energy Conversion, Stiftstr. 34-36, 45470 Mülheim/Ruhr, Germany