Experimental aspects of polarization optimized experiments (POE) for magic angle spinning solid-state NMR of microcrystalline and membrane-bound proteins

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Scopus citations

Abstract

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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages37-53
Number of pages17
DOIs
StatePublished - Jan 1 2018

Publication series

NameMethods in Molecular Biology
Volume1688
ISSN (Print)1064-3745

Keywords

  • DUMAS
  • MAeSTOSO
  • MEIOSIS
  • Multiple acquisitions
  • POE
  • SIM-CP
  • Solid-state NMR

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