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

T. Gopinath, Gianluigi Veglia

Research output: Chapter in Book/Report/Conference proceedingChapter

10 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 - 2018

Publication series

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

Bibliographical note

Publisher Copyright:
© 2018, Springer Science+Business Media LLC.

Keywords

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

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