Adiabatic TOBSY in rotating solids.
A MAS solid state NMR approach for achieving efficient scalar coupling mediated through-bond (13)C chemical shift correlations of the aliphatic carbons in uniformly labelled peptides/proteins is described. The method involves the application of a continuous train of adiabatic inversion pulses, as in the adiabatic TOCSY experiments carried out in solution state NMR studies. While rotor synchronised application of adiabatic inversion pulses leads to dipolar correlations, it is shown here via numerical simulations and experimental measurements that asynchronous application of adiabatic pulses can facilitate the mapping of through-bond connectivities. The method employs a suitable phasing scheme for generating the desired isotropic mixing Hamiltonian and requires moderate (13)C RF field strength only.
Leppert
Jörg
J
Abteilung Molekulare Biophysik/NMR-Spektroskopie, Institut für Molekulare Biotechnologie, 07745 Jena, Germany.
Ohlenschläger
Oliver
O
Görlach
Matthias
M
Ramachandran
Ramadurai
R
D002247:Carbon Isotopes / Q000737:chemistry*; D003198:Computer Simulation; D008962:Models, Theoretical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*
D002247:Carbon Isotopes