Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection |
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Authors: | Duma Luminita Hediger Sabine Brutscher Bernhard Böckmann Anja Emsley Lyndon |
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Affiliation: | Laboratoire de Chimie, UMR 5532 CNRS/ENS, Ecole Normale Supérieure de Lyon, 69364 Lyon, France. |
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Abstract: | 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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