---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
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abstract:
- lang: eng
  text: Protein conformational energy landscapes are shaped not only by intramolecular
    interactions but also by their environment. In protein crystals and protein–protein
    complexes, intermolecular contacts alter this energy landscape, but the exact
    nature of this alteration is difficult to decipher. Understanding how the crystal
    lattice affects protein dynamics is crucial for crystallography-based studies
    of motion, yet its influence on collective motions remains unclear. Aromatic ring
    flips in the hydrophobic core represent sensitive probes of such dynamics. Here,
    we compare the kinetics of aromatic ring flips in the protein GB1 in crystals,
    in complex with its binding partner IgG, and in solution, combining advanced isotope
    labelling with quantitative NMR methods. We show that rings in the core flip nearly
    a thousand times less frequently in crystals than in solution. Enhanced-sampling
    molecular dynamics simulations, based on a crystal structure of a GB1 variant
    reported in this work, reproduce these elevated barriers and reveal how the crystal
    restrains motions.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: We thank N. R. Skrynnikov and O. O. Lebedenko (St. Petersburg) for
  insightful discussions and for performing exploratory MD simulations. We are grateful
  to T. Schubeis (Lyon) for advice on GB1 crystallization and R. Schmid for initial
  crystallization trials. We thank C. Mueller-Dieckmann for assistance with room-temperature
  X-ray crystallography data collection on beamline ID30B at the ESRF, which is acknowledged
  for providing beamtime through its In-House Research programme. We thank S. Falkner
  for assistance with constructing the structural model of the IgG:GB1 complex. We
  thank J. Lewandowski for providing feedback on the paper and granting access to
  backbone relaxation data of IgG:GB1T2Q and GB1T2Q microcrystals. This research was
  supported by the Scientific Service Units (SSU) of the Institute of Science and
  Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance
  and the Lab Support Facilities. We thank P. Rovó and M. V. Falcón for excellent
  support of the NMR facility. L.M.B. is recipient of a DOC fellowship of the Austrian
  Academy of Sciences at the Institute of Science and Technology Austria (grant number
  PR10660EAW01). C.C. acknowledges the European Research Council (grant project 101097272
  ‘MilliInMicro’) and the Métropole du Grand Nancy (grant project ‘ARC’). BM07-FIP2
  is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under
  grant agreement ANR-21-ESRE-0011.Open access funding provided by Institute of Science
  and Technology (IST Austria).
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Lea Marie
  full_name: Becker, Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
- first_name: Haohao
  full_name: Fu, Haohao
  last_name: Fu
- first_name: Benjamin
  full_name: Tatman, Benjamin
  id: 71cda2f3-e604-11ee-a1df-da10587eda3f
  last_name: Tatman
- first_name: Matthias
  full_name: Dreydoppel, Matthias
  last_name: Dreydoppel
- first_name: Anna
  full_name: Kapitonova, Anna
  id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
  last_name: Kapitonova
- first_name: Daniel
  full_name: Balazs, Daniel
  id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E
  last_name: Balazs
  orcid: 0000-0001-7597-043X
- first_name: Ulrich
  full_name: Weininger, Ulrich
  last_name: Weininger
- first_name: Sylvain
  full_name: Engilberge, Sylvain
  last_name: Engilberge
- first_name: Christophe
  full_name: Chipot, Christophe
  last_name: Chipot
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein
    dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026;18:1221-1230.
    doi:<a href="https://doi.org/10.1038/s41557-026-02155-0">10.1038/s41557-026-02155-0</a>
  apa: Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs,
    D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics
    in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href="https://doi.org/10.1038/s41557-026-02155-0">https://doi.org/10.1038/s41557-026-02155-0</a>
  chicago: Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna
    Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot,
    and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in
    Crystals and Complexes.” <i>Nature Chemistry</i>. Springer Nature, 2026. <a href="https://doi.org/10.1038/s41557-026-02155-0">https://doi.org/10.1038/s41557-026-02155-0</a>.
  ieee: L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein
    dynamics in crystals and complexes,” <i>Nature Chemistry</i>, vol. 18. Springer
    Nature, pp. 1221–1230, 2026.
  ista: Becker LM, Fu H, Tatman B, Dreydoppel M, Kapitonova A, Balazs D, Weininger
    U, Engilberge S, Chipot C, Schanda P. 2026. Aromatic ring flips reveal reshaping
    of protein dynamics in crystals and complexes. Nature Chemistry. 18, 1221–1230.
  mla: Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein
    Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, vol. 18, Springer
    Nature, 2026, pp. 1221–30, doi:<a href="https://doi.org/10.1038/s41557-026-02155-0">10.1038/s41557-026-02155-0</a>.
  short: L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U.
    Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry 18 (2026) 1221–1230.
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: The cryo and room-temperature crystal structures of GB1QDD
  are deposited at the PDB under the access codes 9I2I and 9T8Z, respectively. The
  solid-state NMR backbone assignment of GB1QDD is deposited at the BMRB under the
  access code 53330. NMR spectra, analysis scripts and raw data are publicly available
  at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-20641)120. Files
  to reproduce the enhanced-sampling MD simulations are publicly available at the
  ISTA research explorer (https://doi.org/10.15479/AT-ISTA-21145)121.
date_created: 2026-06-21T22:03:01Z
date_published: 2026-07-01T00:00:00Z
date_updated: 2026-08-04T09:32:45Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
- _id: LifeSc
doi: 10.1038/s41557-026-02155-0
external_id:
  pmid:
  - '42271006'
file:
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intvolume: '        18'
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month: '07'
oa: 1
oa_version: Published Version
page: 1221-1230
pmid: 1
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
  grant_number: '26777'
  name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
    approaches
publication: Nature Chemistry
publication_identifier:
  eissn:
  - '17554349'
  issn:
  - '17554330'
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
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    url: https://ista.ac.at/en/news/how-proteins-breathe/
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    status: public
researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes
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: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 18
year: '2026'
...
---
_id: '19696'
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
article_processing_charge: No
author:
- first_name: Benjamin
  full_name: Tatman, Benjamin
  id: 71cda2f3-e604-11ee-a1df-da10587eda3f
  last_name: Tatman
citation:
  ama: 'Tatman B. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion
    in the Solid State.” 2025. doi:<a href="https://doi.org/10.15479/AT-ISTA-19696">10.15479/AT-ISTA-19696</a>'
  apa: 'Tatman, B. (2025). Dataset for “Bumps on the Road: The Way to Clean Relaxation
    Dispersion in the Solid State.” Institute of Science and Technology Austria. <a
    href="https://doi.org/10.15479/AT-ISTA-19696">https://doi.org/10.15479/AT-ISTA-19696</a>'
  chicago: 'Tatman, Benjamin. “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation
    Dispersion in the Solid State.’” Institute of Science and Technology Austria,
    2025. <a href="https://doi.org/10.15479/AT-ISTA-19696">https://doi.org/10.15479/AT-ISTA-19696</a>.'
  ieee: 'B. Tatman, “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion
    in the Solid State.’” Institute of Science and Technology Austria, 2025.'
  ista: 'Tatman B. 2025. Dataset for ‘Bumps on the Road: The Way to Clean Relaxation
    Dispersion in the Solid State’, Institute of Science and Technology Austria, <a
    href="https://doi.org/10.15479/AT-ISTA-19696">10.15479/AT-ISTA-19696</a>.'
  mla: 'Tatman, Benjamin. <i>Dataset for “Bumps on the Road: The Way to Clean Relaxation
    Dispersion in the Solid State.”</i> Institute of Science and Technology Austria,
    2025, doi:<a href="https://doi.org/10.15479/AT-ISTA-19696">10.15479/AT-ISTA-19696</a>.'
  short: B. Tatman, (2025).
contributor:
- contributor_type: project_leader
  first_name: Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- contributor_type: researcher
  first_name: Vidhyalakshmi
  last_name: Sridharan
- contributor_type: researcher
  first_name: Motilal
  last_name: Uttarkabat
- contributor_type: researcher
  first_name: Christopher
  last_name: Jaroniec
- contributor_type: researcher
  first_name: Matthias
  last_name: Ernst
- contributor_type: researcher
  first_name: Petra
  id: c316e53f-b965-11eb-b128-bb26acc59c00
  last_name: Rovo
  orcid: 0000-0001-8729-7326
corr_author: '1'
date_created: 2025-05-14T10:46:07Z
date_published: 2025-07-31T00:00:00Z
date_updated: 2026-06-10T08:33:41Z
day: '31'
department:
- _id: PaSc
doi: 10.15479/AT-ISTA-19696
file:
- access_level: open_access
  checksum: 4c2d29404e070bda7d5619f728ec555c
  content_type: application/zip
  creator: btatman
  date_created: 2025-07-31T08:14:40Z
  date_updated: 2025-07-31T08:14:40Z
  file_id: '20094'
  file_name: dataset.zip
  file_size: 557878455
  relation: main_file
  success: 1
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  checksum: 6cbccd602be0ecb6ddb1f81fdfcadf92
  content_type: text/plain
  creator: btatman
  date_created: 2025-07-31T08:14:21Z
  date_updated: 2025-07-31T08:14:21Z
  file_id: '20095'
  file_name: readme.txt
  file_size: 3514
  relation: main_file
  success: 1
file_date_updated: 2025-07-31T08:14:40Z
has_accepted_license: '1'
month: '07'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
  link:
  - description: Paper to which the dataset corresponds.
    relation: research_paper
    url: http.//doi.org/10.1021/jacs.5c09057
  record:
  - id: '20321'
    relation: research_data
    status: public
status: public
title: 'Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in
  the Solid State"'
tmp:
  image: /images/cc_by_nc_sa.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
    BY-NC-SA 4.0)
  short: CC BY-NC-SA (4.0)
type: research_data
user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20321'
abstract:
- lang: eng
  text: Microsecond-to-millisecond motions are instrumental for many biomolecular
    functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation
    Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique
    for studying these dynamic processes. While BMRD experiments are routinely used
    to probe protein motions in solution, the experiment is more demanding in the
    solid state, where dipolar couplings complicate the spin dynamics. It is believed
    that high deuteration levels are required and sufficient to obtain accurate and
    quantitative data. Here we show that even under fast magic-angle spinning and
    high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common.
    The origin of these artifacts is identified as a second-order three-spin Mixed
    Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts
    are found to be a significant confounding factor for the accurate quantification
    of microsecond protein dynamics using BMRD in the solid state. We show that the
    application of low-power continuous wave (CW) decoupling simultaneously with the
    15N spin-lock leads to the suppression of these conditions and enables quantitative
    measurements of microsecond exchange in the solid state. Remarkably, the application
    of decoupling allows the measurement of accurate BMRD even in fully protonated
    proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements
    in MAS NMR.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: The authors thank Alexey Krushelnitsky for useful discussions. C.P.J.
  thanks NSF (MCB-2303862) and NIH (R35GM156238 and S10OD012303) for funding. 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 and the Lab Support Facilities.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Benjamin
  full_name: Tatman, Benjamin
  id: 71cda2f3-e604-11ee-a1df-da10587eda3f
  last_name: Tatman
- first_name: Vidhyalakshmi
  full_name: Sridharan, Vidhyalakshmi
  last_name: Sridharan
- first_name: Motilal
  full_name: Uttarkabat, Motilal
  last_name: Uttarkabat
- first_name: Christopher P.
  full_name: Jaroniec, Christopher P.
  last_name: Jaroniec
- first_name: Matthias
  full_name: Ernst, Matthias
  last_name: Ernst
- first_name: Petra
  full_name: Rovo, Petra
  id: c316e53f-b965-11eb-b128-bb26acc59c00
  last_name: Rovo
  orcid: 0000-0001-8729-7326
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Tatman B, Sridharan V, Uttarkabat M, et al. Bumps on the road: The way to
    clean relaxation dispersion magic-angle spinning NMR. <i>Journal of the American
    Chemical Society</i>. 2025;147(32):29315-29326. doi:<a href="https://doi.org/10.1021/jacs.5c09057">10.1021/jacs.5c09057</a>'
  apa: 'Tatman, B., Sridharan, V., Uttarkabat, M., Jaroniec, C. P., Ernst, M., Rovo,
    P., &#38; Schanda, P. (2025). Bumps on the road: The way to clean relaxation dispersion
    magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/jacs.5c09057">https://doi.org/10.1021/jacs.5c09057</a>'
  chicago: 'Tatman, Benjamin, Vidhyalakshmi Sridharan, Motilal Uttarkabat, Christopher
    P. Jaroniec, Matthias Ernst, Petra Rovo, and Paul Schanda. “Bumps on the Road:
    The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” <i>Journal of
    the American Chemical Society</i>. American Chemical Society, 2025. <a href="https://doi.org/10.1021/jacs.5c09057">https://doi.org/10.1021/jacs.5c09057</a>.'
  ieee: 'B. Tatman <i>et al.</i>, “Bumps on the road: The way to clean relaxation
    dispersion magic-angle spinning NMR,” <i>Journal of the American Chemical Society</i>,
    vol. 147, no. 32. American Chemical Society, pp. 29315–29326, 2025.'
  ista: 'Tatman B, Sridharan V, Uttarkabat M, Jaroniec CP, Ernst M, Rovo P, Schanda
    P. 2025. Bumps on the road: The way to clean relaxation dispersion magic-angle
    spinning NMR. Journal of the American Chemical Society. 147(32), 29315–29326.'
  mla: 'Tatman, Benjamin, et al. “Bumps on the Road: The Way to Clean Relaxation Dispersion
    Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>, vol.
    147, no. 32, American Chemical Society, 2025, pp. 29315–26, doi:<a href="https://doi.org/10.1021/jacs.5c09057">10.1021/jacs.5c09057</a>.'
  short: B. Tatman, V. Sridharan, M. Uttarkabat, C.P. Jaroniec, M. Ernst, P. Rovo,
    P. Schanda, Journal of the American Chemical Society 147 (2025) 29315–29326.
corr_author: '1'
date_created: 2025-09-10T05:37:19Z
date_published: 2025-08-01T00:00:00Z
date_updated: 2026-06-10T08:33:41Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
- _id: NMR
doi: 10.1021/jacs.5c09057
external_id:
  isi:
  - '001542746200001'
  pmid:
  - '40748291'
file:
- access_level: open_access
  checksum: b350d56ddddefea96cebd62c277c0ff5
  content_type: application/pdf
  creator: dernst
  date_created: 2025-09-10T07:53:10Z
  date_updated: 2025-09-10T07:53:10Z
  file_id: '20337'
  file_name: 2025_JACS_Tatman.pdf
  file_size: 5235353
  relation: main_file
  success: 1
file_date_updated: 2025-09-10T07:53:10Z
has_accepted_license: '1'
intvolume: '       147'
isi: 1
issue: '32'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
page: 29315-29326
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
  eissn:
  - 1520-5126
  issn:
  - 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
related_material:
  record:
  - id: '19696'
    relation: used_in_publication
    status: public
scopus_import: '1'
status: public
title: 'Bumps on the road: The way to clean relaxation dispersion magic-angle spinning
  NMR'
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 147
year: '2025'
...
---
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'
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