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Old 11-24-2010, 09:16 PM
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Default Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u

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

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

J Am Chem Soc. 2003 Oct 1;125(39):11816-7

Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L

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.

PMID: 14505393 [PubMed - indexed for MEDLINE]



Source: PubMed
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