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Cited by 31Advanced NMR Techniques and ApplicationsElectron Spin Resonance StudiesProtein Structure and Dynamics

1H-detected characterization of carbon–carbon networks in highly flexible protonated biomolecules using MAS NMR

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Bahri, Salima, Safeer, Adil, Adler, Agnes, Smedes, Hanneke, van Ingen, Hugo, Baldus, Marc·2023·Journal of Biomolecular NMR
DOI 10.1007/s10858-023-00415-6PMC PMC10307723
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Abstract

In the last three decades, the scope of solid-state NMR has expanded to exploring complex biomolecules, from large protein assemblies to intact cells at atomic-level resolution. This diversity in macromolecules frequently features highly flexible components whose insoluble environment precludes the use of solution NMR to study their structure and interactions. While High-resolution Magic-Angle Spinning (HR-MAS) probes offer the capacity for gradient-based 1 H-detected spectroscopy in solids, such probes are not commonly used for routine MAS NMR experiments. As a result, most exploration of the flexible regime entails either 13 C-detected experiments, the use of partially perdeuterated systems, or ultra-fast MAS. Here we explore proton-detected pulse schemes probing through-bond 13 C–13 C networks to study mobile protein sidechains as well as polysaccharides in a broadband manner. We demonstrate the use of such schemes to study a mixture of microtubule-associated protein (MAP) tau and human microtubules (MTs), and the cell wall of the fungus Schizophyllum commune using 2D and 3D spectroscopy, to show its viability for obtaining unambiguous correlations using standard fast-spinning MAS probes at high and ultra-high magnetic fields.

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  • Extending to a 3D hCCH TOCSY experiment with DIPSI-3 mixing allowed the resolution of all carbon sites, revealing five distinct 1,2-linked mannose forms, three glucopyranose forms from β-1,3-glucan in the cell walls, five forms of galactose or glucose derivatives, such as glucose-phosphates, alongside α- and β-glucoses in the media.

    “Extending to a 3D hCCH TOCSY experiment with DIPSI-3 mixing73 allowed the resolution of all carbon sites (Supplementary Table 2), revealing five distinct 1,2-linked mannose forms (Fig. 2d), three glucopyranose forms from β-1,3-glucan (Fig. 2e) in the cell walls, five forms of galactose or glucose derivatives, such as glucose-phosphates (Fig. 2e)74, alongside α- and β-glucoses in the media (Fig. 2g”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [73]

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Cited by

Sorted by citations

Authors
Bahri, S., Safeer, A., Adler, A., Smedes, H., van Ingen, H., & Baldus, M.
Affiliations
Utrecht University (NL)
Corresponding author
  • Bahri, Salima
  • Baldus, Marc
ORCID
Venue
Journal of Biomolecular NMR
Publisher
Springer Science and Business Media LLC
Published
2023-06
Volume
77
Issue
3
Pages
111-119
ISSN
  • 0925-2738 (ISSN-L)
  • 1573-5001
DOI
10.1007/s10858-023-00415-6
PMC
PMC10307723
OpenAlex
W4379768210
Cited by
31
References
0
Citations by year
2026: 7 · 2025: 13 · 2024: 7 · 2023: 4
FWCI
2.86
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biomolecular NMR (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
Funders
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek,Netherlands (184.035.002)
  • Horizon 2020 Framework Programme (FUNGAR; project 58132)
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek (718.015.001)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
proton-detected NMR, polysaccharides, tau protein, microtubules, high-resolution magic angle spinning, ultrahigh magnetic fields
MeSH terms
Carbon, Humans, Magnetic Resonance Imaging, Magnetic Resonance Spectroscopy, Proteins, Protons, Nuclear Magnetic Resonance, Biomolecular

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