Evidence map›Paper›PMID 26440131›Full record

ArticleSolid state nuclear magnetic resonance2015

Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.

Jonathan K Williams, Klaus Schmidt-Rohr, Mei Hong

Abstract read
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Article in Solid state nuclear magnetic resonance, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

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16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Improved spectral resolution of [Journal of biomolecular NMR · 2023
    Article
  8. Article
  9. Review
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  11. Article
  12. De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  13. Article
  14. Direct amideJournal of biomolecular NMR · 2018
    Article
  15. Review
  16. Journal of biomolecular NMR · 2017
    Article
4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Jonathan K WilliamsDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States.
Klaus Schmidt-RohrDepartment of Chemistry, Brandeis University, Waltham, MA 02453, United States.
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States. Electronic address: meihong@mit.edu.

Funding

Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024
$4.8M
NIGMS NIH HHS GM088204NIGMS NIH HHS R01 GM088204
6 · The paper itself

Abstract

The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play important roles in biology through π-π and cation-π interactions. To better resolve and assign aromatic residues' (13)C signals in magic-angle-spinning (MAS) solid-state NMR spectra, we introduce two spectral editing techniques. The first method uses gated (1)H decoupling in a proton-driven spin-diffusion (PDSD) experiment to remove all protonated (13)C signals and retain only non-protonated carbon signals in the aromatic region of the (13)C spectra. The second technique uses chemical shift filters and (1)H-(13)C dipolar dephasing to selectively detect the Cα, Cβ and CO cross peaks of aromatic residues while suppressing the signals of all aliphatic residues. We demonstrate these two techniques on amino acids, a model peptide, and the microcrystalline protein GB1, and show that they significantly simplify the 2D NMR spectra and both reveal and permit the ready assignment of the aromatic residues' signals.

Indexed as

Magnetic PhenomenaMagnetic Resonance SpectroscopyModels, MolecularNitrogen IsotopesProtein ConformationProteinsNitrogen IsotopesProteinsAromatic residuesASSETGated decouplingPDSD

Identifiers

PMID26440131
PMCPMC4674322

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.