Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy View Full Text


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Article Info

DATE

2012-09-18

AUTHORS

Donghua H. Zhou, Andrew J. Nieuwkoop, Deborah A. Berthold, Gemma Comellas, Lindsay J. Sperling, Ming Tang, Gautam J. Shah, Elliott J. Brea, Luisel R. Lemkau, Chad M. Rienstra

ABSTRACT

Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the site-specific resonance assignment. Here we demonstrate resonance assignments based on high-sensitivity proton-detected three-dimensional experiments for samples of different physical states, including a fully-protonated small protein (GB1, 6 kDa), a deuterated microcrystalline protein (DsbA, 21 kDa), a membrane protein (DsbB, 20 kDa) prepared in a lipid environment, and the extended core of a fibrillar protein (α-synuclein, 14 kDa). In our implementation of these experiments, including CONH, CO(CA)NH, CANH, CA(CO)NH, CBCANH, and CBCA(CO)NH, dipolar-based polarization transfer methods have been chosen for optimal efficiency for relatively high protonation levels (full protonation or 100 % amide proton), fast magic-angle spinning conditions (40 kHz) and moderate proton decoupling power levels. Each H–N pair correlates exclusively to either intra- or inter-residue carbons, but not both, to maximize spectral resolution. Experiment time can be reduced by at least a factor of 10 by using proton detection in comparison to carbon detection. These high-sensitivity experiments are especially important for membrane proteins, which often have rather low expression yield. Proton-detection based experiments are expected to play an important role in accelerating protein structure elucidation by solid-state NMR with the improved sensitivity and resolution. More... »

PAGES

291-305

References to SciGraph publications

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  • 2011-07-31. Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion in JOURNAL OF BIOMOLECULAR NMR
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  • 2011-12-14. Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers in JOURNAL OF BIOMOLECULAR NMR
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  • 2004-02. A Selective Intra-HN(CA)CO Experiment for the Backbone Assignment of Deuterated Proteins in JOURNAL OF BIOMOLECULAR NMR
  • 2007-09-26. Temperature-dependent sensitivity enhancement of solid-state NMR spectra of α-synuclein fibrils in JOURNAL OF BIOMOLECULAR NMR
  • 2010-03-16. Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state in JOURNAL OF BIOMOLECULAR NMR
  • 2010-02. Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10858-012-9672-z

    DOI

    http://dx.doi.org/10.1007/s10858-012-9672-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1045126691

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/22986689


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