Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
 

Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra


Abstract We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically optimised symmetry-based mixing sequences and the simultaneous recording of chemical shift correlation spectra such as: 3D NCAC and 3D NHH with dual receivers, 3D NCâ?²C and 3D Câ?²NCA with sequential 13C acquisitions, 3D NHH and 3D NCâ?²H with sequential 1H acquisitions and 3D CANH and 3D Câ??NH with broadband 13Câ??15N mixing are demonstrated using microcrystalline samples of the β1 immunoglobulin binding domain of protein G (GB1) and the chicken α-spectrin SH3 domain.

• Content Type Journal Article
• Category Communication
• Pages 1-11
• DOI 10.1007/s10858-012-9680-z
• Authors
  • Peter Bellstedt, Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany
  • Christian Herbst, Department of Physics, Faculty of Science, Ubon Ratchathani University, Ubon Ratchathani, 34190 Thailand
  • Sabine Häfner, Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany
  • Jörg Leppert, Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany
  • Matthias Görlach, Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany
  • Ramadurai Ramachandran, Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738

Source: Journal of Biomolecular NMR