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Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
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Protein sample preparation for solid-state NMR investigations.

Denis Lacabanne1, Marie-Laure Fogeron2, Thomas Wiegand3

  • 1Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon, 69367 Lyon, France; Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland.

Progress in Nuclear Magnetic Resonance Spectroscopy
|February 27, 2019
PubMed
Summary
This summary is machine-generated.

Solid-state NMR sample preparation requires stable isotope labeling and specialized reconstitution for membrane proteins. Advanced techniques enable structural studies of large proteins and small sample amounts.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Solid-state NMR (SSNMR) sample preparation shares similarities with solution-state NMR, notably the need for stable isotope labeling.
  • Investigating membrane proteins using SSNMR necessitates adapted membrane reconstitution schemes.
  • Specialized schemes involving metal ions and radicals are required for dynamic nuclear polarization and paramagnetic NMR in solids.

Purpose of the Study:

  • To review specific aspects of protein sample preparation for solid-state NMR.
  • To highlight techniques enabling structural investigations of challenging biological systems.
  • To discuss advancements facilitating the study of large proteins and complexes.

Main Methods:

  • Stable isotope labeling for protein samples.
  • Membrane reconstitution schemes for native lipid environments.
  • Dynamic nuclear polarization and paramagnetic NMR techniques.
  • Sample sedimentation for rotor filling in magic-angle spinning (MAS) NMR.
  • Selective, unselective, and segmental labeling strategies.
  • Cell-free protein expression for sub-milligram sample amounts.

Main Results:

  • SSNMR allows investigation of membrane proteins in native lipids.
  • Advanced techniques like dynamic nuclear polarization and paramagnetic NMR are applicable.
  • Sample sedimentation enables structural studies of previously inaccessible objects.
  • SSNMR can analyze very large proteins and complexes without significant line broadening.
  • Fast MAS techniques allow investigation of sub-milligram protein amounts.

Conclusions:

  • Solid-state NMR sample preparation involves specialized techniques beyond solution-state NMR.
  • The reviewed methods expand the scope of structural biology, enabling studies of diverse and challenging biomolecular systems.
  • Advancements in SSNMR sample preparation are crucial for understanding protein structure and dynamics.