title: 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 NC'C and 3D C'NCA with sequential (13)C acquisitions, 3D NHH and 3D NC'H with sequential (1)H acquisitions and 3D CANH and 3D C'NH with broadband (13)C-(15)N mixing are demonstrated using microcrystalline samples of the β1 immunoglobulin binding domain of protein G (GB1) and the chicken α-spectrin SH3 domain.
authors.affiliation: Biomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, Jena, Germany.
authors.forename: Peter
authors.initials: P
authors.lastname: Bellstedt
authors.forename: Christian
authors.initials: C
authors.lastname: Herbst
authors.forename: Sabine
authors.initials: S
authors.lastname: Häfner
authors.forename: Jörg
authors.initials: J
authors.lastname: Leppert
authors.forename: Matthias
authors.initials: M
authors.lastname: Görlach
authors.forename: Ramadurai
authors.initials: R
authors.lastname: Ramachandran
mesh_terms: D002247:Carbon Isotopes; D005583:Fourier Analysis; D009419:Nerve Tissue Proteins / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D013049:Spectrin / Q000737:chemistry; D018909:src Homology Domains
chemical_list: D002247:Carbon Isotopes; C029152:G-substrate; D009419:Nerve Tissue Proteins; D009587:Nitrogen Isotopes; D011506:Proteins; D013049:Spectrin