---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20258'
abstract:
- lang: eng
  text: The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise
    deuterated proteins holds great potential for high-resolution solution and magic-angle
    spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues
    play key roles for example at active sites of enzymes. Taking advantage of a chemically
    synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we
    demonstrate here the usefulness of proton-detected MAS NMR approaches to probe
    arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric
    enzyme malate dehydrogenase we detected a wide range of motions, from sites that
    are rigid on time scales of at least tens of milliseconds to residues undergoing
    predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements
    enabled quantitative determination of these dynamics. We observed microsecond
    dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to
    sample different β-turn conformations on this time scale. The labeling scheme
    and experiments presented here expand the toolkit for high-resolution proton-detected
    MAS NMR.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: This work was supported financially by the Austrian Science Fund
  (FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific
  Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through
  resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support
  Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent
  support of the NMR facility.
article_number: '169379'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Darja
  full_name: Rohden, Darja
  id: 81dc668a-19fa-11f0-bf31-d56534059ef3
  last_name: Rohden
- first_name: Federico
  full_name: Napoli, Federico
  id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
  last_name: Napoli
  orcid: 0000-0002-9043-136X
- first_name: Anna
  full_name: Kapitonova, Anna
  id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
  last_name: Kapitonova
- first_name: Benjamin
  full_name: Tatman, Benjamin
  id: 71cda2f3-e604-11ee-a1df-da10587eda3f
  last_name: Tatman
- first_name: Roman J.
  full_name: Lichtenecker, Roman J.
  last_name: Lichtenecker
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine
    dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme.
    <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href="https://doi.org/10.1016/j.jmb.2025.169379">10.1016/j.jmb.2025.169379</a>
  apa: Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38;
    Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with
    a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.jmb.2025.169379">https://doi.org/10.1016/j.jmb.2025.169379</a>
  chicago: Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman
    J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning
    NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>.
    Elsevier, 2025. <a href="https://doi.org/10.1016/j.jmb.2025.169379">https://doi.org/10.1016/j.jmb.2025.169379</a>.
  ieee: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P.
    Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific
    isotope-labeling scheme,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23.
    Elsevier, 2025.
  ista: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025.
    Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
    scheme. Journal of Molecular Biology. 437(23), 169379.
  mla: Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR
    with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>,
    vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href="https://doi.org/10.1016/j.jmb.2025.169379">10.1016/j.jmb.2025.169379</a>.
  short: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda,
    Journal of Molecular Biology 437 (2025).
corr_author: '1'
date_created: 2025-08-31T22:01:33Z
date_published: 2025-12-01T00:00:00Z
date_updated: 2026-08-13T14:19:01Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1016/j.jmb.2025.169379
external_id:
  isi:
  - '001618289100020'
file:
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  date_created: 2025-12-29T14:51:40Z
  date_updated: 2025-12-29T14:51:40Z
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file_date_updated: 2025-12-29T14:51:40Z
fulldoi: https://doi.org/10.1016/j.jmb.2025.169379
has_accepted_license: '1'
intvolume: '       437'
isi: 1
issue: '23'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
  grant_number: I05812
  name: AlloSpace. The emergence and mechanisms of allostery
publication: Journal of Molecular Biology
publication_identifier:
  eissn:
  - 1089-8638
  issn:
  - 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
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  - id: '19956'
    relation: research_data
    status: public
scopus_import: '1'
status: public
title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
  scheme
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 437
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...