13C-detected through-bond correlation experiments for protein resonance assignment by ultra-fast MAS solid-state NMR. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue ChemPhysChem Année : 2013

13C-detected through-bond correlation experiments for protein resonance assignment by ultra-fast MAS solid-state NMR.

Résumé

We present two sequences which combine ((1)H,(15)N) and ((15)N,(13)C) selective cross-polarization steps with an efficient variant of the J-based homonuclear transfer scheme, in which a spin-state-selective (S(3)E) block is incorporated to improve both resolution and sensitivity in the direct (13)C dimension. We propose these two sequences as a part of a suite of four N-C correlation experiments allowing for the assignment of protein backbone resonances in the solid state. We illustrate these experiments under ultra-fast magic angle spinning conditions on two samples of microcrystalline dimeric human superoxide dismutase (SOD, 153×2 amino acids), in its diamagnetic ("empty", Zn(II)) and paramagnetic (Cu(II), Zn(II)) states.

Dates et versions

hal-00915846 , version 1 (09-12-2013)

Identifiants

Citer

Emeline Barbet-Massin, Andrew J. Pell, Michael J. Knight, Amy L. Webber, Isabella C Felli, et al.. 13C-detected through-bond correlation experiments for protein resonance assignment by ultra-fast MAS solid-state NMR.. ChemPhysChem, 2013, 14 (13), pp.3131-3137. ⟨10.1002/cphc.201201097⟩. ⟨hal-00915846⟩
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