Our research is focused on solid-state NMR of macroscopically aligned samples including membrane proteins. A particular advantage of the method is in being able to measure dipolar couplings between the neighboring spin sites which is made possible by the defined sample orientation. The angular-dependent dipolar couplings can be extracted using the so-called separated local-field (SLF) pulse sequences and their variants, and provide direct input for structure determination. The SLF method can be expanded to include internuclear correlations, spectroscopic assignment, and spectral editing.
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