---
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OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '21777'
abstract:
- lang: eng
text: The advantageous characteristics attributed to the 19F nucleus have made it
a popular target for nuclear magnetic resonance (NMR) once again in recent years.
Aside from solution NMR, an increasing number of studies have been conducted applying
solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here,
the high chemical shift anisotropy and strong dipolar couplings can be utilised
to get structural insights into proteins and measure long distances. Despite increasing
popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR
often suffers from slow longitudinal T1 relaxation and therefore long recycle
delays. In this work, we expand paramagnetic doping, an approach commonly used
to reduce proton T1 relaxation times, to 19F-labelled biological samples. We study
the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation
in a [5-19F13C]-tryptophan-labelled protein via 19F-detected MAS NMR experiments.
The observed paramagnetic relaxation enhancement substantially reduces measurement
times of 19F MAS NMR experiments without compromising resolution. Additionally,
we report the chemical shift assignments of all four fluorotryptophan signals
in the 12×39 kDa-large protein TET2 using a mutagenesis approach.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: We thank Ben P. Tatman for insightful discussions. This research
was supported by the Scientific Service Units (SSUs) of ISTA through resources provided
by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. We thank
Prof. Tobias Madl (Medical University Graz) for a sample of Omniscan. Lea M. Becker
is the recipient of a DOC fellowship of the Austrian Academy of Sciences at the
Institute of Science and Technology Austria (grant no. PR10660EAW01).
article_processing_charge: Yes
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: Giorgia
full_name: Toscano, Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Rajkumar
full_name: Singh, Rajkumar
id: a3089acd-6806-11ee-bacc-f0c7d500ad20
last_name: Singh
- first_name: Undina
full_name: Guillerm, Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- 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: Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle
spinning NMR with paramagnetic dopants. Magnetic Resonance. 2026;7(1):29-37.
doi:10.5194/mr-7-29-2026
apa: Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker,
R. J., & Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning
NMR with paramagnetic dopants. Magnetic Resonance. Copernicus Publications.
https://doi.org/10.5194/mr-7-29-2026
chicago: Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina
Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular
Magic-Angle Spinning NMR with Paramagnetic Dopants.” Magnetic Resonance.
Copernicus Publications, 2026. https://doi.org/10.5194/mr-7-29-2026.
ieee: L. M. Becker et al., “Accelerated 19F biomolecular magic-angle spinning
NMR with paramagnetic dopants,” Magnetic Resonance, vol. 7, no. 1. Copernicus
Publications, pp. 29–37, 2026.
ista: Becker LM, Toscano G, Kapitonova A, Singh R, Guillerm U, Lichtenecker RJ,
Schanda P. 2026. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic
dopants. Magnetic Resonance. 7(1), 29–37.
mla: Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning
NMR with Paramagnetic Dopants.” Magnetic Resonance, vol. 7, no. 1, Copernicus
Publications, 2026, pp. 29–37, doi:10.5194/mr-7-29-2026.
short: L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker,
P. Schanda, Magnetic Resonance 7 (2026) 29–37.
corr_author: '1'
date_created: 2026-05-03T22:01:36Z
date_published: 2026-04-16T00:00:00Z
date_updated: 2026-05-07T06:49:59Z
day: '16'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.5194/mr-7-29-2026
external_id:
pmid:
- '42057802'
has_accepted_license: '1'
intvolume: ' 7'
issue: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
main_file_link:
- open_access: '1'
url: https://doi.org/10.5194/mr-7-29-2026
month: '04'
oa: 1
oa_version: Published Version
page: 29-37
pmid: 1
project:
- _id: B67AFEDC-15C9-11EA-A837-991A96BB2854
name: IST Austria Open Access Fund
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publication: Magnetic Resonance
publication_identifier:
eissn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants
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: 7
year: '2026'
...
---
OA_place: publisher
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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. Nature Chemistry. 2026. doi:10.1038/s41557-026-02155-0
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. Nature Chemistry. Springer Nature. https://doi.org/10.1038/s41557-026-02155-0
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.” Nature Chemistry. Springer Nature, 2026. https://doi.org/10.1038/s41557-026-02155-0.
ieee: L. M. Becker et al., “Aromatic ring flips reveal reshaping of protein
dynamics in crystals and complexes,” Nature Chemistry. Springer Nature,
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.
mla: Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein
Dynamics in Crystals and Complexes.” Nature Chemistry, Springer Nature,
2026, doi:10.1038/s41557-026-02155-0.
short: L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U.
Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry (2026).
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: 2026-06-10T00:00:00Z
date_updated: 2026-06-24T08:47:58Z
day: '10'
ddc:
- '540'
department:
- _id: PaSc
- _id: LifeSc
doi: 10.1038/s41557-026-02155-0
external_id:
pmid:
- '42271006'
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41557-026-02155-0
month: '06'
oa: 1
oa_version: Published Version
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: epub_ahead
publisher: Springer Nature
quality_controlled: '1'
related_material:
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relation: research_data
status: public
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relation: research_data
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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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2026'
...
---
_id: '21145'
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
labeling 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 new crystal structure, reproduce these
elevated barriers and reveal how the crystal restrains motions. '
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: "We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg)
for insightful discussions and for performing exploratory MD simulations. We are
grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca
Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance
with constructing the structural model of the IgG:GB1 complex.\r\nThis 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. We thank Petra Rovó and Margarita Valhondo Falcón
for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC
fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology
Austria (grant no. PR10660EAW01). Christophe Chipot 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."
article_processing_charge: No
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: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
citation:
ama: Becker LM, Schanda P, Chipot C. Additional Data for “Aromatic Ring Flips Reveal
Reshaping of Protein Dynamics in Crystals and Complexes.” 2026. doi:10.15479/AT-ISTA-21145
apa: Becker, L. M., Schanda, P., & Chipot, C. (2026). Additional Data for “Aromatic
Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute
of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-21145
chicago: Becker, Lea Marie, Paul Schanda, and Christophe Chipot. “Additional Data
for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and
Complexes.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-21145.
ieee: L. M. Becker, P. Schanda, and C. Chipot, “Additional Data for ‘Aromatic Ring
Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute
of Science and Technology Austria, 2026.
ista: Becker LM, Schanda P, Chipot C. 2026. Additional Data for ‘Aromatic Ring Flips
Reveal Reshaping of Protein Dynamics in Crystals and Complexes’, Institute of
Science and Technology Austria, 10.15479/AT-ISTA-21145.
mla: Becker, Lea Marie, et al. Additional Data for “Aromatic Ring Flips Reveal
Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science
and Technology Austria, 2026, doi:10.15479/AT-ISTA-21145.
short: L.M. Becker, P. Schanda, C. Chipot, (2026).
contributor:
- contributor_type: researcher
first_name: Haohao
last_name: Fu
- contributor_type: researcher
first_name: Benjamin
id: 71cda2f3-e604-11ee-a1df-da10587eda3f
last_name: Tatman
- contributor_type: researcher
first_name: Matthias
last_name: Dreydoppel
- contributor_type: researcher
first_name: Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- contributor_type: researcher
first_name: Daniel
id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E
last_name: Balazs
orcid: 0000-0001-7597-043X
- contributor_type: researcher
first_name: Ulrich
last_name: Weininger
- contributor_type: researcher
first_name: Sylvain
last_name: Engilberge
corr_author: '1'
date_created: 2026-02-05T13:54:39Z
date_published: 2026-02-09T00:00:00Z
date_updated: 2026-06-24T08:47:57Z
day: '09'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT-ISTA-21145
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checksum: 02a419cce8cea450bc952f35488d2df5
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date_created: 2026-02-05T13:52:37Z
date_updated: 2026-02-05T13:52:37Z
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month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publisher: Institute of Science and Technology Austria
related_material:
record:
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relation: earlier_version
status: public
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relation: used_in_publication
status: public
status: public
title: Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics
in Crystals and Complexes"
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
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short: CC BY-NC (4.0)
type: research_data
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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
labeling 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 new crystal structure, reproduce these
elevated barriers and reveal how the crystal restrains motions. '
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: "We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg)
for insightful discussions and for performing exploratory MD simulations. We are
grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca
Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance
with constructing the structural model of the IgG:GB1 complex.\r\nThis 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. We thank Petra Rovó and Margarita Valhondo Falcón
for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC
fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology
Austria (grant no. PR10660EAW01). Christophe Chipot 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."
article_processing_charge: No
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: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Becker LM, Schanda P. Data for “Aromatic Ring Flips Reveal Reshaping of Protein
Dynamics in Crystals and Complexes.” 2025. doi:10.15479/AT-ISTA-20641
apa: Becker, L. M., & Schanda, P. (2025). Data for “Aromatic Ring Flips Reveal
Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science
and Technology Austria. https://doi.org/10.15479/AT-ISTA-20641
chicago: Becker, Lea Marie, and Paul Schanda. “Data for ‘Aromatic Ring Flips Reveal
Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science
and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20641.
ieee: L. M. Becker and P. Schanda, “Data for ‘Aromatic Ring Flips Reveal Reshaping
of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology
Austria, 2025.
ista: Becker LM, Schanda P. 2025. Data for ‘Aromatic Ring Flips Reveal Reshaping
of Protein Dynamics in Crystals and Complexes’, Institute of Science and Technology
Austria, 10.15479/AT-ISTA-20641.
mla: Becker, Lea Marie, and Paul Schanda. Data for “Aromatic Ring Flips Reveal
Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science
and Technology Austria, 2025, doi:10.15479/AT-ISTA-20641.
short: L.M. Becker, P. Schanda, (2025).
contributor:
- contributor_type: researcher
first_name: 'Haohao '
last_name: Fu
- contributor_type: researcher
first_name: Benjamin
id: 71cda2f3-e604-11ee-a1df-da10587eda3f
last_name: Tatman
- contributor_type: researcher
first_name: Matthias
last_name: Dreydoppel
- contributor_type: researcher
first_name: Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- contributor_type: researcher
first_name: Daniel
id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E
last_name: Balazs
orcid: 0000-0001-7597-043X
- contributor_type: researcher
first_name: Ulrich
last_name: Weininger
- contributor_type: researcher
first_name: Sylvain
last_name: Engilberge
- contributor_type: researcher
first_name: Christophe
last_name: Chipot
corr_author: '1'
date_created: 2025-11-13T09:29:58Z
date_published: 2025-11-18T00:00:00Z
date_updated: 2026-06-24T08:47:57Z
day: '18'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT-ISTA-20641
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creator: lbecker
date_created: 2025-11-17T11:54:17Z
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file_name: README.pdf
file_size: 191376
relation: table_of_contents
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month: '11'
oa: 1
oa_version: Published Version
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '21145'
relation: later_version
status: public
- id: '22105'
relation: used_in_publication
status: public
status: public
title: Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals
and Complexes"
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: research_data
user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d
year: '2025'
...
---
_id: '17161'
abstract:
- lang: eng
text: Dynamic processes in molecules can occur on a wide range of timescales, and
it is important to understand which timescales of motion contribute to different
parameters used in dynamics measurements. For spin relaxation, this can easily
be understood from the sampling frequencies of the spectral-density function by
different relaxation-rate constants. In addition to data from relaxation measurements,
determining dynamically averaged anisotropic interactions in magic-angle spinning
(MAS) solid-state NMR allows for better quantification of the amplitude of molecular
motion. For partially averaged anisotropic interactions, the relevant timescales
of motion are not so clearly defined. Whether the averaging depends on the experimental
methods (e.g., pulse sequences) or conditions (e.g., MAS frequency, magnitude
of anisotropic interaction, radio-frequency field amplitudes) is not fully understood.
To investigate these questions, we performed numerical simulations of dynamic
systems based on the stochastic Liouville equation using several experiments for
recoupling the dipolar coupling, chemical-shift anisotropy or quadrupolar coupling.
As described in the literature, the transition between slow motion, where parameters
characterizing the anisotropic interaction are not averaged, and fast motion,
where the tensors are averaged leading to a scaled anisotropic quantity, occurs
over a window of motional rate constants that depends mainly on the strength of
the interaction. This transition region can span 2 orders of magnitude in exchange-rate
constants (typically in the microsecond range) but depends only marginally on
the employed recoupling scheme or sample spinning frequency. The transition region
often coincides with a fast relaxation of coherences, making precise quantitative
measurements difficult. Residual couplings in off-magic-angle experiments, however,
average over longer timescales of motion. While in principle one may gain information
on the timescales of motion from the transition area, extracting such information
is hampered by low signal-to-noise ratio in experimental spectra due to fast relaxation
that occurs in the same region.
acknowledgement: "We would like to thank Kay Saalwächter for pointing out important
aspects of the intermediate regime during the open review process. Lea Marie Becker
is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute
of Science and Technology Austria.\r\nThis research has been supported by the Österreichischen
Akademie der Wissenschaften (grant no. PR10660EAW01) and the Schweizerischer Nationalfonds
zur Förderung der Wissenschaftlichen Forschung (grant nos. 200020_188988 and 200020_219375)."
article_processing_charge: Yes
article_type: original
author:
- first_name: Kathrin
full_name: Aebischer, Kathrin
last_name: Aebischer
- 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: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
citation:
ama: Aebischer K, Becker LM, Schanda P, Ernst M. Evaluating the motional timescales
contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic
Resonance. 2024;5(1):69-86. doi:10.5194/mr-5-69-2024
apa: Aebischer, K., Becker, L. M., Schanda, P., & Ernst, M. (2024). Evaluating
the motional timescales contributing to averaged anisotropic interactions in MAS
solid-state NMR. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-5-69-2024
chicago: Aebischer, Kathrin, Lea Marie Becker, Paul Schanda, and Matthias Ernst.
“Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions
in MAS Solid-State NMR.” Magnetic Resonance. Copernicus Publications, 2024.
https://doi.org/10.5194/mr-5-69-2024.
ieee: K. Aebischer, L. M. Becker, P. Schanda, and M. Ernst, “Evaluating the motional
timescales contributing to averaged anisotropic interactions in MAS solid-state
NMR,” Magnetic Resonance, vol. 5, no. 1. Copernicus Publications, pp. 69–86,
2024.
ista: Aebischer K, Becker LM, Schanda P, Ernst M. 2024. Evaluating the motional
timescales contributing to averaged anisotropic interactions in MAS solid-state
NMR. Magnetic Resonance. 5(1), 69–86.
mla: Aebischer, Kathrin, et al. “Evaluating the Motional Timescales Contributing
to Averaged Anisotropic Interactions in MAS Solid-State NMR.” Magnetic Resonance,
vol. 5, no. 1, Copernicus Publications, 2024, pp. 69–86, doi:10.5194/mr-5-69-2024.
short: K. Aebischer, L.M. Becker, P. Schanda, M. Ernst, Magnetic Resonance 5 (2024)
69–86.
date_created: 2024-06-23T22:01:02Z
date_published: 2024-06-11T00:00:00Z
date_updated: 2025-06-11T13:26:12Z
day: '11'
ddc:
- '530'
department:
- _id: PaSc
doi: 10.5194/mr-5-69-2024
external_id:
pmid:
- '40384772'
file:
- access_level: open_access
checksum: d01074f6919387fcaf8c9ebed320ccae
content_type: application/pdf
creator: dernst
date_created: 2024-06-27T06:42:55Z
date_updated: 2024-06-27T06:42:55Z
file_id: '17181'
file_name: 2024_MagneticResonance_Aebischer.pdf
file_size: 6736194
relation: main_file
success: 1
file_date_updated: 2024-06-27T06:42:55Z
has_accepted_license: '1'
intvolume: ' 5'
issue: '1'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: 69-86
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: Magnetic Resonance
publication_identifier:
eissn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Evaluating the motional timescales contributing to averaged anisotropic interactions
in MAS solid-state 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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2024'
...