Resolution Enhancement in Multidimensional Solid-State NMR Spectroscopy of Proteins Using Spin-State Selection

• Published in: Journal of the American Chemical Society 2003-10, Vol.125 (39), p.11816-11817
• Main Authors: Duma, Luminita, Hediger, Sabine, Brutscher, Bernhard, Böckmann, Anja, Emsley, Lyndon
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Biochemistry, Molecular Biology; Biological and medical sciences; Carbon Isotopes; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Life Sciences; Nuclear Magnetic Resonance, Biomolecular - methods; Phosphoproteins - chemistry; Proteins; Proteins - chemistry
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja036893n

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−Cα correlation experiment, applied to a microcrystalline 85-residue protein. With this new sequence, all four components of the CO−Cα 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−Cα spectrum compared to a standard spin-diffusion experiment. The new technique also allows an easy distinction between “direct” and “relayed” transfer cross-peaks.