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Cited by 193Advanced NMR Techniques and ApplicationsElectron Spin Resonance StudiesNMR spectroscopy and applications

Broadband homonuclear correlation spectroscopy driven by combined R2nv sequences under fast magic angle spinning for NMR structural analysis of organic and biological solids

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Hou, Guangjin, Yan, Si, Trébosc, Julien, Amoureux, Jean-Paul, Polenova, Tatyana·2013·Journal of Magnetic Resonance
DOI 10.1016/j.jmr.2013.04.009PMC PMC3703537
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Abstract

We recently described a family of experiments for R2n(v) Driven Spin Diffusion (RDSD) spectroscopy suitable for homonuclear correlation experiments under fast MAS conditions [G. Hou, S. Yan, S.J. Sun, Y. Han, I.J. Byeon, J. Ahn, J. Concel, A. Samoson, A.M. Gronenborn, T. Polenova, Spin diffusion drive by R-symmetry sequencs: applications to homonuclear correlation spectroscopy in MAS NMR of biological and organic solids, J. Am. Chem. Soc. 133 (2011) 3943-3953]. In these RDSD experiments, since the broadened second-order rotational resonance conditions are dominated by the radio frequency field strength and the phase shifts, as well as the size of reintroduced dipolar couplings, the different R2n(v) sequences display unique polarization transfer behaviors and different recoupling frequency bandwidths. Herein, we present a series of modified R2n(v) sequences, dubbed COmbined R2n(v)-Driven (CORD), that yield broadband homonuclear dipolar recoupling and give rise to uniform distribution of cross peak intensities across the entire correlation spectrum. We report NMR experiments and numerical simulations demonstrating that these CORD spin diffusion sequences are suitable for broadband recoupling at a wide range of magnetic fields and MAS frequencies, including fast-MAS conditions (νr=40 kHz and above). Since these CORD sequences are largely insensitive to dipolar truncation, they are well suited for the determination of long-range distance constraints, which are indispensable for the structural characterization of a broad range of systems. Using U-(13)C,(15)N-alanine and U-(13)C,(15)N-histidine, we show that under fast-MAS conditions, the CORD sequences display polarization transfer efficiencies within broadband frequency regions that are generally higher than those offered by other existing spin diffusion pulse schemes. A 89-residue U-(13)C,(15)N-dynein light chain (LC8) protein has also been used to demonstrate that the CORD sequences exhibit uniformly high cross peak intensities across the entire chemical shift range.

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  • Compared to PDSD, CORD provides higher efficiency due to the use of active recoupling pulses.

    “Compared to proton-driven spin diffusion (PDSD), CORD provides higher efficiency due to the use of active recoupling pulses113.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [113]

    The Introduction says conventional PDSD deteriorates as MAS frequency rises and does not work above about 25–30 kHz. The Results and Discussion describe CORD’s applied recoupling pulses and its broadband polarization transfer at fast MAS. This supports the comparison under fast-MAS conditions, but not the sentence’s unqualified claim that CORD is more efficient than PDSD generally. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • CORD efficiently drives homonuclear 13C-13C polarization transfer under fast MAS conditions and high magnetic fields.

    “CORD efficiently drives homonuclear 13C-13C polarization transfer under fast MAS conditions and high magnetic fields113.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [113]

  • At the slower MAS rate of 13.5 kHz used in this study, CORD's performance is comparable to that of DARR, while offering the advantage of lower radiofrequency power requirements during the recoupling period.

    “At the slower MAS rate of 13.5 kHz used in this study, its performance is comparable to that of Dipolar-Assisted Rotational Resonance (DARR), while offering the advantage of lower radiofrequency power requirements during the recoupling period.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [113]

    The Introduction identifies DARR as a conventional method used at MAS rates of 30 kHz or lower, while the Methods report CORD experiments at 40 kHz. Neither those passages nor the searched Results passages compare CORD with DARR at 13.5 kHz or establish a lower recoupling-period RF power requirement for CORD. Searched for DARR, 13.5 kHz, and RF-power comparisons. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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Authors
Hou, G., Yan, S., Trébosc, J., Amoureux, J.-P., & Polenova, T.
Affiliations
  • University of Pittsburgh (US)
  • University of Delaware (US)
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Hou, Guangjin
  • Polenova, Tatyana
ORCID
Venue
Journal of Magnetic Resonance
Publisher
Elsevier BV
Published
2013-07
Volume
232
Pages
18-30
ISSN
1090-7807 (ISSN-L)
DOI
10.1016/j.jmr.2013.04.009
PMC
PMC3703537
OpenAlex
W2067520392
Cited by
193
References
0
Citations by year
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FWCI
2.09
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Journal of Magnetic Resonance (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • HAL (submittedVersion)
Funders
  • the National Institutes of Health
  • R01GM085396 and 8P30GM103519-03
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
  • Physical Sciences › Physics and Astronomy › Nuclear and High Energy Physics › NMR spectroscopy and applications
Keywords
fast magic angle spinning, polarization transfer, alanine, histidine, protein structure determination
MeSH terms
Algorithms, Carbon Isotopes, Magnetic Resonance Imaging, Models, Chemical, Proteins, Nuclear Magnetic Resonance, Biomolecular, Molecular Dynamics Simulation

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