Conventional NMR pulse sequences record one spectrum per experiment, while spending most of the time waiting for the spin system to return to the equilibrium. As a result, a full set of multidimensional NMR experiments for biological macromolecules may take up to several months to complete. Here, we present a practical guide for setting up a new class of MAS solid-state NMR experiments (POE or polarization optimized experiments) that enable the simultaneous acquisition of multiple spectra of proteins, accelerating data acquisition. POE exploit the long-lived 15N polarization of isotopically labeled proteins and enable one to obtain up to eight spectra, by concatenating classical NMR pulse sequences. This new strategy propels data throughput of solid-state NMR spectroscopy of fibers, microcrystalline preparations, as well as membrane proteins.
CITATION STYLE
Gopinath, T., & Veglia, G. (2018). Experimental aspects of polarization optimized experiments (POE) for magic angle spinning solid-state NMR of microcrystalline and membrane-bound proteins. In Methods in Molecular Biology (Vol. 1688, pp. 37–53). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7386-6_2
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