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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.

Come in and explore what we’ve been up to these days!