---
OA_place: repository
OA_type: free access
_id: '21284'
abstract:
- lang: eng
text: The advantageous characteristics attributed to the 19F nucleus have made it
a popular target for NMR once again in recent years. Aside from solution NMR,
an increasing number of studies have been conducted applying solid-state magic-angle-spinning
NMR to fluorine-labeled samples. Here, the high chemical shift anisotropy and
strong dipolar couplings can be utilized 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-labeled
biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F and
13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labeled 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 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 (SSU) of Institute of Science and
Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance
Facility and the Lab Support Facility.
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. Research data for “Accelerated 19F biomolecular magic-angle
spinning NMR with paramagnetic dopants.” 2026. doi:10.15479/AT-ISTA-21284
apa: Becker, L. M., & Schanda, P. (2026). Research data for “Accelerated 19F
biomolecular magic-angle spinning NMR with paramagnetic dopants.” Institute of
Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-21284
chicago: Becker, Lea Marie, and Paul Schanda. “Research Data for ‘Accelerated 19F
Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.’” Institute of
Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-21284.
ieee: L. M. Becker and P. Schanda, “Research data for ‘Accelerated 19F biomolecular
magic-angle spinning NMR with paramagnetic dopants.’” Institute of Science and
Technology Austria, 2026.
ista: Becker LM, Schanda P. 2026. Research data for ‘Accelerated 19F biomolecular
magic-angle spinning NMR with paramagnetic dopants’, Institute of Science and
Technology Austria, 10.15479/AT-ISTA-21284.
mla: Becker, Lea Marie, and Paul Schanda. Research Data for “Accelerated 19F
Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” Institute
of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-21284.
short: L.M. Becker, P. Schanda, (2026).
contributor:
- contributor_type: researcher
first_name: Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- contributor_type: researcher
first_name: Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- contributor_type: researcher
first_name: Rajkumar
id: a3089acd-6806-11ee-bacc-f0c7d500ad20
last_name: Singh
- contributor_type: researcher
first_name: Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- contributor_type: researcher
first_name: Roman
last_name: Lichtenecker
corr_author: '1'
date_created: 2026-02-17T10:17:14Z
date_published: 2026-02-18T00:00:00Z
date_updated: 2026-06-10T09:28:41Z
day: '18'
ddc:
- '541'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT-ISTA-21284
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date_created: 2026-02-17T10:11:14Z
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file_id: '21286'
file_name: README.txt
file_size: 1993
relation: table_of_contents
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fulldoi: https://doi.org/10.15479/AT-ISTA-21284
has_accepted_license: '1'
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '2'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
status: public
title: Research data for "Accelerated 19F biomolecular magic-angle spinning NMR with
paramagnetic dopants"
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: '2026'
...
---
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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: 2026-07-20T09:49:12Z
day: '16'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.5194/mr-7-29-2026
external_id:
pmid:
- '42057802'
fulldoi: https://doi.org/10.5194/mr-7-29-2026
has_accepted_license: '1'
intvolume: ' 7'
issue: '1'
language:
- iso: eng
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'
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status: public
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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)
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type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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year: '2026'
...
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abstract:
- lang: eng
text: "Characterizing protein dynamics at the atomic level is essential for our
understanding of biological mechanisms. Whether it is to facilitate metabolite
transport, catalyze reactions, transmit signals, or regulate metabolism – proteins
are constantly in motion and sample multiple conformational states to fulfill
their function. Nuclear magnetic resonance (NMR) spectroscopy is particularly
well suited to elucidate the dynamics of biomolecules on their complex free-energy
landscape. In particular, solid-state magic-angle spinning (MAS) NMR enables the
study of large molecular assemblies, protein crystals, or insoluble proteins at
atomic resolution without an inherent molecular size limitation. MAS NMR experiments
to probe protein dynamics are extremely versatile and sensitive to motional timescales
from picoseconds to seconds. Over the past decades, technological advances, developments
in experimental design, and new isotope-labeling approaches have further expanded
the possibilities of this technique and significantly improved the accuracy of
the determined motional parameters.\r\nFunctionally important sites of proteins
often contain aromatic residues. Their side-chain motions have therefore long
served as valuable indicators of mechanistically relevant dynamics in NMR studies.
In this thesis, site-specifically labeled aromatic residues act as sensitive reporters
for MAS NMR studies of protein dynamics. The first part addresses how different
environments impact side-chain motion by probing ring flips of phenylalanines
and tyrosines in crystalline proteins and amyloid fibrils. It provides important
insights for the analysis of dynamics obtained in non-native protein environments
and emphasizes the complex factors that determine the timescale of internal dynamics.
In the second part, the focus shifts towards methodological questions regarding
the investigation of protein dynamics by 19F MAS NMR. The fluorine nucleus exhibits
promising characteristics for NMR studies but also presents significant challenges,
which is why the full methodological potential of 19F MAS NMR has not been fully
realized yet. This work demonstrates that paramagnetic doping can considerably
reduce the measurement time and improve the sensitivity of fluorinated samples.
Finally, 19F MAS NMR is evaluated as a tool for studying protein side-chain dynamics
on the example of tryptophans. The results illustrate the challenges in analyzing
such experiments and lay the foundation for further development of 19F MAS NMR
relaxation studies.\r\nTaken together, this thesis highlights the potential of
combining specific isotope labeling, MAS NMR, and complementary methods such as
crystallography and computational simulations to elucidate internal protein dynamics.
The further development of such integrative approaches will be crucial to improving
our understanding of complex mechanisms and protein function.\r\n"
acknowledged_ssus:
- _id: LifeSc
- _id: NMR
acknowledgement: "During the work on this thesis, I was the recipient of a DOC Fellowship
of the Austrian\r\nAcademy of Sciences at the Institute of Science and Technology
Austria (grant no. PR10660EAW01)."
alternative_title:
- ISTA Thesis
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
citation:
ama: Becker LM. Exploring protein dynamics using specific labeling approaches for
solid-state MAS NMR. 2026. doi:10.15479/AT-ISTA-22334
apa: Becker, L. M. (2026). Exploring protein dynamics using specific labeling
approaches for solid-state MAS NMR. Institute of Science and Technology Austria.
https://doi.org/10.15479/AT-ISTA-22334
chicago: Becker, Lea Marie. “Exploring Protein Dynamics Using Specific Labeling
Approaches for Solid-State MAS NMR.” Institute of Science and Technology Austria,
2026. https://doi.org/10.15479/AT-ISTA-22334.
ieee: L. M. Becker, “Exploring protein dynamics using specific labeling approaches
for solid-state MAS NMR,” Institute of Science and Technology Austria, 2026.
ista: Becker LM. 2026. Exploring protein dynamics using specific labeling approaches
for solid-state MAS NMR. Institute of Science and Technology Austria.
mla: Becker, Lea Marie. Exploring Protein Dynamics Using Specific Labeling Approaches
for Solid-State MAS NMR. Institute of Science and Technology Austria, 2026,
doi:10.15479/AT-ISTA-22334.
short: L.M. Becker, Exploring Protein Dynamics Using Specific Labeling Approaches
for Solid-State MAS NMR, Institute of Science and Technology Austria, 2026.
corr_author: '1'
das_tickbox: '1'
date_created: 2026-07-14T08:08:51Z
date_published: 2026-07-13T00:00:00Z
date_updated: 2026-08-04T09:32:45Z
day: '13'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT-ISTA-22334
doi_confirm: '1'
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month: '07'
oa: 1
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grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publication_identifier:
isbn:
- 978-3-99078-084-8
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
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status: public
supervisor:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
title: Exploring protein dynamics using specific labeling approaches for solid-state
MAS NMR
tmp:
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legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: dissertation
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2026'
...
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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. Nature Chemistry. 2026;18:1221-1230.
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, 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.” Nature Chemistry, vol. 18, Springer
Nature, 2026, pp. 1221–30, 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 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
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title: Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes
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...
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_id: '21145'
abstract:
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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:
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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
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id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
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- 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: 2026-08-04T09:32:45Z
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- _id: PaSc
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title: Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics
in Crystals and Complexes"
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_id: '20641'
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: 2026-08-04T09:32:44Z
day: '18'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
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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:
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status: public
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title: Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals
and Complexes"
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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: 2026-09-11T08:49:55Z
day: '11'
ddc:
- '530'
department:
- _id: PaSc
doi: 10.5194/mr-5-69-2024
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- '40384772'
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oa_version: Published Version
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title: Evaluating the motional timescales contributing to averaged anisotropic interactions
in MAS solid-state NMR
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legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
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type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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year: '2024'
...
---
_id: '12497'
abstract:
- lang: eng
text: Aromatic side chains are important reporters of the plasticity of proteins,
and often form important contacts in protein–protein interactions. We studied
aromatic residues in the two structurally homologous cross-β amyloid fibrils HET-s,
and HELLF by employing a specific isotope-labeling approach and magic-angle-spinning
NMR. The dynamic behavior of the aromatic residues Phe and Tyr indicates that
the hydrophobic amyloid core is rigid, without any sign of "breathing motions"
over hundreds of milliseconds at least. Aromatic residues exposed at the fibril
surface have a rigid ring axis but undergo ring flips on a variety of time scales
from nanoseconds to microseconds. Our approach provides direct insight into hydrophobic-core
motions, enabling a better evaluation of the conformational heterogeneity generated
from an NMR structural ensemble of such amyloid cross-β architecture.
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. Research data to: The rigid core and flexible surface
of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic
residues. 2023. doi:10.15479/AT:ISTA:12497'
apa: 'Becker, L. M., & Schanda, P. (2023). Research data to: The rigid core
and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy
of aromatic residues. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12497'
chicago: 'Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core
and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
of Aromatic Residues.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:12497.'
ieee: 'L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible
surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
aromatic residues.” Institute of Science and Technology Austria, 2023.'
ista: 'Becker LM, Schanda P. 2023. Research data to: The rigid core and flexible
surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
aromatic residues, Institute of Science and Technology Austria, 10.15479/AT:ISTA:12497.'
mla: 'Becker, Lea Marie, and Paul Schanda. Research Data to: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
of Aromatic Residues. Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12497.'
short: L.M. Becker, P. Schanda, (2023).
contributor:
- contributor_type: researcher
first_name: Mélanie
last_name: Berbon
- contributor_type: researcher
first_name: Alicia
last_name: Vallet
- contributor_type: researcher
first_name: Axelle
last_name: Grelard
- contributor_type: researcher
first_name: Estelle
last_name: Morvan
- contributor_type: researcher
first_name: Benjamin
last_name: Bardiaux
- contributor_type: researcher
first_name: Roman
last_name: Lichtenecker
- contributor_type: researcher
first_name: Matthias
last_name: Ernst
- contributor_type: researcher
first_name: Antoine
last_name: Loquet
- contributor_type: contact_person
first_name: Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- contributor_type: researcher
first_name: Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
corr_author: '1'
date_created: 2023-02-03T08:08:02Z
date_published: 2023-03-23T00:00:00Z
date_updated: 2024-10-21T06:01:38Z
day: '23'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT:ISTA:12497
file:
- access_level: open_access
checksum: fd9a28620a81a82991fb70f4fd6591d9
content_type: application/zip
creator: lbecker
date_created: 2023-03-23T10:03:16Z
date_updated: 2023-03-24T09:34:20Z
file_id: '12743'
file_name: Research_Data.zip
file_size: 87018103
relation: main_file
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checksum: 30ebdfb600af118fcf8518b6efe0b7e9
content_type: text/plain
creator: dernst
date_created: 2023-03-24T07:13:55Z
date_updated: 2023-03-24T09:42:03Z
file_id: '12755'
file_name: README.txt
file_size: 747
relation: main_file
file_date_updated: 2023-03-24T09:42:03Z
fulldoi: https://doi.org/10.15479/AT:ISTA:12497
has_accepted_license: '1'
keyword:
- aromatic side chains
- isotopic labeling
- protein dynamics
- ring flips
- spin relaxation
month: '03'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '12675'
relation: used_in_publication
status: public
status: public
title: 'Research data to: The rigid core and flexible surface of amyloid fibrils probed
by magic-angle-spinning NMR spectroscopy of aromatic residues'
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '14835'
abstract:
- lang: ger
text: Aromatische Seitenketten sind wichtige Indikatoren für die Plastizität von
Proteinen und bilden oft entscheidende Kontakte bei Protein‐Protein‐Wechselwirkungen.
Wir untersuchten aromatische Reste in den beiden strukturell homologen cross‐β
Amyloidfibrillen HET‐s und HELLF mit Hilfe eines spezifischen Ansatzes zur Isotopenmarkierung
und Festkörper NMR mit Drehung am magischen Winkel. Das dynamische Verhalten der
aromatischen Reste Phe und Tyr deutet darauf hin, dass der hydrophobe Amyloidkern
starr ist und keine Anzeichen von “atmenden Bewegungen” auf einer Zeitskala von
Hunderten von Millisekunden zeigt. Aromatische Reste, die exponiert an der Fibrillenoberfläche
sitzen, haben zwar eine starre Ringachse, weisen aber Ringflips auf verschiedenen
Zeitskalen von Nanosekunden bis Mikrosekunden auf. Unser Ansatz bietet einen direkten
Einblick in die Bewegungen des hydrophoben Kerns und ermöglicht eine bessere Bewertung
der Konformationsheterogenität, die aus einem NMR‐Strukturensemble einer solchen
Cross‐β‐Amyloidstruktur hervorgeht.
acknowledgement: Wir danken Albert A. Smith (Leipzig) für aufschlussreiche Diskussionen.
Diese Arbeit wurde mit Mitteln des Europäischen Forschungsrats (StG-2012-311318
an P.S.) unterstützt und nutzte die Plattformen des Grenoble Instruct-ERIC Center
(ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) im Rahmen der Grenoble Partnership for Structural
Biology (PSB) sowie die Einrichtungen und das Fachwissen der Biophysical and Structural
Chemistry Platform (BPCS) am IECB, CNRS UAR3033, INSERM US001 und der Universität
Bordeaux.
article_number: e202219314
article_processing_charge: Yes (in subscription journal)
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: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- 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, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche
von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen
Resten. Angewandte Chemie. 2023;135(19). doi:10.1002/ange.202219314
apa: Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,
… Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen
– Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte
Chemie. Wiley. https://doi.org/10.1002/ange.202219314
chicago: Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen
– Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” Angewandte
Chemie. Wiley, 2023. https://doi.org/10.1002/ange.202219314.
ieee: L. M. Becker et al., “Der starre Kern und die flexible Oberfläche von
Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,”
Angewandte Chemie, vol. 135, no. 19. Wiley, 2023.
ista: Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. Der starre Kern und die flexible Oberfläche
von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen
Resten. Angewandte Chemie. 135(19), e202219314.
mla: Becker, Lea Marie, et al. “Der starre Kern und die flexible Oberfläche von
Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.”
Angewandte Chemie, vol. 135, no. 19, e202219314, Wiley, 2023, doi:10.1002/ange.202219314.
short: L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).
corr_author: '1'
date_created: 2024-01-18T10:01:01Z
date_published: 2023-05-02T00:00:00Z
date_updated: 2024-10-09T21:07:55Z
day: '02'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1002/ange.202219314
file:
- access_level: open_access
checksum: 98e68d370159f7be52a3d7c8a8ee1198
content_type: application/pdf
creator: dernst
date_created: 2024-01-23T08:57:01Z
date_updated: 2024-01-23T08:57:01Z
file_id: '14876'
file_name: 2023_AngewChem_Becker.pdf
file_size: 1004676
relation: main_file
success: 1
file_date_updated: 2024-01-23T08:57:01Z
fulldoi: https://doi.org/10.1002/ange.202219314
has_accepted_license: '1'
intvolume: ' 135'
issue: '19'
keyword:
- General Medicine
language:
- iso: ger
month: '05'
oa: 1
oa_version: Published Version
publication: Angewandte Chemie
publication_identifier:
eissn:
- 1521-3757
issn:
- 0044-8249
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning
NMR Spektroskopie von aromatischen Resten
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: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 135
year: '2023'
...
---
_id: '14861'
abstract:
- lang: eng
text: Cover Page
article_number: ' e202304138'
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: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- 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, Berbon M, Vallet A, et al. Cover Picture: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy
of Aromatic Residues. Vol 62. Wiley; 2023. doi:10.1002/anie.202304138'
apa: 'Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux,
B., … Schanda, P. (2023). Cover Picture: The rigid core and flexible surface
of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic
residues. Angewandte Chemie International Edition (Vol. 62). Wiley.
https://doi.org/10.1002/anie.202304138'
chicago: 'Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. Cover Picture: The Rigid Core and Flexible Surface of Amyloid
Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues.
Angewandte Chemie International Edition. Vol. 62. Wiley, 2023. https://doi.org/10.1002/anie.202304138.'
ieee: 'L. M. Becker et al., Cover Picture: The rigid core and flexible
surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of
aromatic residues, vol. 62, no. 19. Wiley, 2023.'
ista: 'Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. Cover Picture: The rigid core and flexible
surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of
aromatic residues, Wiley,p.'
mla: 'Becker, Lea Marie, et al. “Cover Picture: The Rigid Core and Flexible Surface
of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic
Residues.” Angewandte Chemie International Edition, vol. 62, no. 19, e202304138,
Wiley, 2023, doi:10.1002/anie.202304138.'
short: 'L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy
of Aromatic Residues, Wiley, 2023.'
corr_author: '1'
date_created: 2024-01-22T11:54:34Z
date_published: 2023-05-02T00:00:00Z
date_updated: 2026-06-18T17:41:09Z
day: '02'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1002/anie.202304138
fulldoi: https://doi.org/10.1002/anie.202304138
intvolume: ' 62'
issue: '19'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/anie.202304138
month: '05'
oa: 1
oa_version: Published Version
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
related_material:
link:
- relation: translation
url: https://doi.org/10.1002/ange.202304138
record:
- id: '12675'
relation: other
status: public
status: public
title: 'Cover Picture: The rigid core and flexible surface of amyloid fibrils probed
by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues'
type: other_academic_publication
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 62
year: '2023'
...
---
_id: '12675'
abstract:
- lang: eng
text: Aromatic side chains are important reporters of the plasticity of proteins,
and often form important contacts in protein--protein interactions. By studying
a pair of structurally homologous cross-β amyloid fibrils, HET-s and HELLF, with
a specific isotope-labeling approach and magic-angle-spinning (MAS) NMR, we have
characterized the dynamic behavior of Phe and Tyr aromatic rings to show that
the hydrophobic amyloid core is rigid, without any sign of "breathing motions"
over hundreds of milliseconds at least. Aromatic residues exposed at the fibril
surface have a rigid ring axis but undergo ring flips, on a variety of time scales
from ns to µs. Our approach provides direct insight into hydrophobic-core motions,
enabling a better evaluation of the conformational heterogeneity generated from
a NMR structural ensemble of such amyloid cross-β architecture.
acknowledgement: We thank AlbertA. Smith (Leipzig)for insightful discussions. This
work was supported by funding from the European Research Council (StG-2012-311318
to P.S.) and used the platforms of the Grenoble Instruct-ERIC center (ISBG;UMS 3518
CNRS-CEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology(PSB) and
facilities and expertiseof the Biophysical and Structural Chemistry platform (BPCS)
at IECB,CNRSUAR3033,INSERMUS001 and Bordeaux University.
article_number: e202219314
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: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- 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, Berbon M, Vallet A, et al. The rigid core and flexible surface of
amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte
Chemie International Edition. 2023;62(19). doi:10.1002/anie.202219314
apa: Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,
… Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed
by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International
Edition. Wiley. https://doi.org/10.1002/anie.202219314
chicago: Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed
by Magic‐Angle Spinning NMR of Aromatic Residues.” Angewandte Chemie International
Edition. Wiley, 2023. https://doi.org/10.1002/anie.202219314.
ieee: L. M. Becker et al., “The rigid core and flexible surface of amyloid
fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” Angewandte
Chemie International Edition, vol. 62, no. 19. Wiley, 2023.
ista: Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. The rigid core and flexible surface of
amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte
Chemie International Edition. 62(19), e202219314.
mla: Becker, Lea Marie, et al. “The Rigid Core and Flexible Surface of Amyloid Fibrils
Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” Angewandte Chemie
International Edition, vol. 62, no. 19, e202219314, Wiley, 2023, doi:10.1002/anie.202219314.
short: L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International
Edition 62 (2023).
corr_author: '1'
date_created: 2023-02-24T10:45:01Z
date_published: 2023-05-01T00:00:00Z
date_updated: 2026-07-20T09:49:12Z
day: '01'
ddc:
- '540'
department:
- _id: GradSch
- _id: PaSc
doi: 10.1002/anie.202219314
external_id:
isi:
- '000956919900001'
pmid:
- '36738230'
file:
- access_level: open_access
checksum: 7dd083ed8850faa55c34e411ed390de9
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T12:33:31Z
date_updated: 2023-08-16T12:33:31Z
file_id: '14072'
file_name: 2023_AngewChemInt_Becker.pdf
file_size: 1422445
relation: main_file
success: 1
file_date_updated: 2023-08-16T12:33:31Z
fulldoi: https://doi.org/10.1002/anie.202219314
has_accepted_license: '1'
intvolume: ' 62'
isi: 1
issue: '19'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
quality_controlled: '1'
related_material:
link:
- description: News on ISTA website
relation: press_release
url: https://ista.ac.at/en/news/dancing-styles-of-atoms/
record:
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relation: research_data
status: public
- id: '14861'
relation: other
status: public
- id: '22334'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle
Spinning NMR of aromatic residues
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: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 62
year: '2023'
...
---
_id: '12114'
abstract:
- lang: eng
text: 'Probing the dynamics of aromatic side chains provides important insights
into the behavior of a protein because flips of aromatic rings in a protein’s
hydrophobic core report on breathing motion involving a large part of the protein.
Inherently invisible to crystallography, aromatic motions have been primarily
studied by solution NMR. The question how packing of proteins in crystals affects
ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning
NMR, advanced phenylalanine 1H-13C/2H isotope labeling and MD simulation to a
protein in three different crystal packing environments to shed light onto possible
impact of packing on ring flips. The flips of the two Phe residues in ubiquitin,
both surface exposed, appear remarkably conserved in the different crystal forms,
even though the intermolecular packing is quite different: Phe4 flips on a ca.
10–20 ns time scale, and Phe45 are broadened in all crystals, presumably due to
µs motion. Our findings suggest that intramolecular influences are more important
for ring flips than intermolecular (packing) effects.'
acknowledgement: The NMR platform in Grenoble is part of the Grenoble Instruct-ERIC
center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural
Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within
the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche)
CBH-EUR-GS (ANR-17-EURE-0003). This work was supported by the European Research
Council (StG-2012-311318-ProtDyn2Function to P.S.) and used the platforms of the
Grenoble Instruct Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI
(ANR-10-INSB-05–02) and GRAL (ANR-10-LABX-49–01) within the Grenoble Partnership
for Structural Biology (PSB). We would like to thank Sergei Izmailov for developing
and maintaining the pyxmolpp2 library. N.R.S. acknowledges support from St. Petersburg
State University in a form of the grant 92425251 and the access to the MRR, MCT
and CAMR resource centers. P.S. thanks Malcolm Levitt for pointing out the fact
that “tensor asymmetry” is better called “tensor biaxiality”.
article_number: '100079'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Olga O.
full_name: Lebedenko, Olga O.
last_name: Lebedenko
- 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: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Nikolai R.
full_name: Skrynnikov, Nikolai R.
last_name: Skrynnikov
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently
packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural
Biology: X. 2023;7. doi:10.1016/j.yjsbx.2022.100079'
apa: 'Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R.,
Skrynnikov, N. R., & Schanda, P. (2023). Aromatic ring flips in differently
packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural
Biology: X. Elsevier. https://doi.org/10.1016/j.yjsbx.2022.100079'
chicago: 'Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman
Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in
Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” Journal
of Structural Biology: X. Elsevier, 2023. https://doi.org/10.1016/j.yjsbx.2022.100079.'
ieee: 'D. F. Gauto et al., “Aromatic ring flips in differently packed ubiquitin
protein crystals from MAS NMR and MD,” Journal of Structural Biology: X,
vol. 7. Elsevier, 2023.'
ista: 'Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR,
Schanda P. 2023. Aromatic ring flips in differently packed ubiquitin protein crystals
from MAS NMR and MD. Journal of Structural Biology: X. 7, 100079.'
mla: 'Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin
Protein Crystals from MAS NMR and MD.” Journal of Structural Biology: X,
vol. 7, 100079, Elsevier, 2023, doi:10.1016/j.yjsbx.2022.100079.'
short: 'D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R.
Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).'
corr_author: '1'
date_created: 2023-01-12T11:55:38Z
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title: Aromatic ring flips in differently packed ubiquitin protein crystals from MAS
NMR and MD
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---
_id: '14036'
abstract:
- lang: eng
text: Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing
itself as a powerful method for the characterization of protein dynamics at the
atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore
microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling,
and pulse sequence design has paved the way for quantitative analyses of even
rare structural fluctuations. In addition to isotropic chemical-shift fluctuations
exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has
a wider arsenal of observables, allowing to see motions even if the exchanging
states do not differ in their chemical shifts. We demonstrate the potential of
the technique for probing motions in challenging large enzymes, membrane proteins,
and protein assemblies.
acknowledgement: We thank Petra Rovó for critical reading of this manuscript. We acknowledge
the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding
by the Institute of Science and Technology Austria.
article_number: '102660'
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author:
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- 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: Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning
relaxation dispersion NMR. Current Opinion in Structural Biology. 2023;82(10).
doi:10.1016/j.sbi.2023.102660
apa: Napoli, F., Becker, L. M., & Schanda, P. (2023). Protein dynamics detected
by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural
Biology. Elsevier. https://doi.org/10.1016/j.sbi.2023.102660
chicago: Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics
Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” Current Opinion
in Structural Biology. Elsevier, 2023. https://doi.org/10.1016/j.sbi.2023.102660.
ieee: F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle
spinning relaxation dispersion NMR,” Current Opinion in Structural Biology,
vol. 82, no. 10. Elsevier, 2023.
ista: Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle
spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10),
102660.
mla: Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning
Relaxation Dispersion NMR.” Current Opinion in Structural Biology, vol.
82, no. 10, 102660, Elsevier, 2023, doi:10.1016/j.sbi.2023.102660.
short: F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology
82 (2023).
corr_author: '1'
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2025-04-14T09:10:17Z
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grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Current Opinion in Structural Biology
publication_identifier:
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quality_controlled: '1'
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title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
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...