Three-dimensional experiment for solid-state NMR of aligned protein samples in high field magnets |
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Authors: | Alexander A. Nevzorov Sang Ho Park Stanley J. Opella |
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Affiliation: | (1) Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, San Diego, CA 92093-0307, USA |
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Abstract: | A pulse sequence that yields three-dimensional 1H chemical shift / 1H-15N heteronuclear dipolar coupling / 15N chemical shift solid-state NMR spectra is demonstrated on a uniformly 15N labeled membrane protein in magnetically aligned phospholipid bilayers. Based on SAMPI4, the pulse sequence yields high resolution in all three dimensions at a 1H resonance frequency of 900 MHz with the relatively low rf field strength (33 kHz) available for a lossy aqueous sample with a commercial spectrometer and probe. The 1H chemical shift frequency dimension is shown to select among amide resonances, which will be useful in studies of larger polytopic membrane proteins where the resonances overlap in two-dimensional spectra. Moreover, the 1H chemical shift, which can be measured from these spectra, provides an additional orientationally dependent frequency as input for structure calculations. Both Alexander A. Nevzorov and Sang Ho Park contributed equally to this work. |
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Keywords: | Bicelle Membrane protein Aligned sample Protein structure |
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