Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of the American Chemical Society Année : 2003

Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.

Résumé

We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer techniques. The selection and transfer of single states allow the removal of the J-coupling contribution from the line width in both the direct and indirect spectral dimensions. This is demonstrated with a new spin-state-selective CO-Calpha correlation experiment, applied to a microcrystalline 85-residue protein. With this new sequence, all four components of the CO-Calpha cross-peaks are separated into different spectra, obtained by linear combination of four recorded data sets. Line narrowing of up to 44% was obtained on the protein sample for the spin-state-selective CO-Calpha spectrum compared to a standard spin-diffusion experiment. The new technique also allows an easy distinction between "direct" and "relayed" transfer cross-peaks.We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer techniques. The selection and transfer of single states allow the removal of the J-coupling contribution from the line width in both the direct and indirect spectral dimensions. This is demonstrated with a new spin-state-selective CO-Calpha correlation experiment, applied to a microcrystalline 85-residue protein. With this new sequence, all four components of the CO-Calpha cross-peaks are separated into different spectra, obtained by linear combination of four recorded data sets. Line narrowing of up to 44% was obtained on the protein sample for the spin-state-selective CO-Calpha spectrum compared to a standard spin-diffusion experiment. The new technique also allows an easy distinction between "direct" and "relayed" transfer cross-peaks.
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Dates et versions

hal-00314370 , version 1 (27-08-2008)

Identifiants

  • HAL Id : hal-00314370 , version 1
  • PUBMED : 14505393

Citer

L. Duma, Sabine Hediger, B. Brutscher, A. Bockmann, L. Emsley. Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.. Journal of the American Chemical Society, 2003, 125, pp.11816-11817. ⟨hal-00314370⟩
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