---
OA_place: publisher
OA_type: gold
_id: '21437'
abstract:
- lang: eng
text: Altermagnets are a class of collinear magnets that exhibit non-relativistic
spin splitting (NRSS) of electronic bands in the absence of net magnetization.
Their potential to generate large spin polarization without spin-orbit coupling
has created strong interest in probes that access the underlying order parameter
directly. In this Perspective, we show that linear magneto-birefringence (LMB)
provides a natural and broadly applicable route to detecting altermagnetic order.
Building on the correspondence between the momentum-space structure of NRSS and
the ferroic ordering of magnetic multipoles in real space, we demonstrate how
$d$-wave and $g$-wave NRSS textures yield distinct LMB responses. We present a
symmetry-based framework that identifies the optical geometries and field configurations
required to isolate specific multipole components, enabling domain imaging and
providing benchmarks for theoretical models of LMB.
acknowledgement: We thank Nicola Spaldin and Marc Vila for valuable discussions. J.O.
received support from the Quantum Materials (KC2202) program under the U.S. Department
of Energy, Office of Science, Office of Basic Energy Sciences, Materials Sciences
and Engineering Division under Contract No. DE-AC02-05CH11231, and the Gordon and
Betty Moore Foundation's EPiQS Initiative through Grant GBMF4537 to J.O. at UC Berkeley.
article_processing_charge: Yes
article_type: original
arxiv: 1
author:
- first_name: Veronika
full_name: Sunko, Veronika
id: 23cb1cf6-2c7a-11ef-91a4-f72fc19f20b3
last_name: Sunko
orcid: 0000-0003-2724-3523
- first_name: J.
full_name: Orenstein, J.
last_name: Orenstein
citation:
ama: Sunko V, Orenstein J. Linear magneto-birefringence as a probe of altermagnetism.
npj Quantum Materials. 2026. doi:10.1038/s41535-026-00901-8
apa: Sunko, V., & Orenstein, J. (2026). Linear magneto-birefringence as a probe
of altermagnetism. Npj Quantum Materials. Springer Nature. https://doi.org/10.1038/s41535-026-00901-8
chicago: Sunko, Veronika, and J. Orenstein. “Linear Magneto-Birefringence as a Probe
of Altermagnetism.” Npj Quantum Materials. Springer Nature, 2026. https://doi.org/10.1038/s41535-026-00901-8.
ieee: V. Sunko and J. Orenstein, “Linear magneto-birefringence as a probe of altermagnetism,”
npj Quantum Materials. Springer Nature, 2026.
ista: Sunko V, Orenstein J. 2026. Linear magneto-birefringence as a probe of altermagnetism.
npj Quantum Materials.
mla: Sunko, Veronika, and J. Orenstein. “Linear Magneto-Birefringence as a Probe
of Altermagnetism.” Npj Quantum Materials, Springer Nature, 2026, doi:10.1038/s41535-026-00901-8.
short: V. Sunko, J. Orenstein, Npj Quantum Materials (2026).
corr_author: '1'
date_created: 2026-03-11T10:40:08Z
date_published: 2026-05-30T00:00:00Z
date_updated: 2026-06-24T10:31:05Z
day: '30'
ddc:
- '530'
department:
- _id: VeSu
doi: 10.1038/s41535-026-00901-8
external_id:
arxiv:
- '2511.16421'
has_accepted_license: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41535-026-00901-8
month: '05'
oa: 1
oa_version: Published Version
publication: npj Quantum Materials
publication_identifier:
eissn:
- 2397-4648
publication_status: epub_ahead
publisher: Springer Nature
status: public
title: Linear magneto-birefringence as a probe of altermagnetism
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
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(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2026'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '22101'
abstract:
- lang: eng
text: "Evolutionary biology examines how the genetic and phenotypic composition\r\nof
populations changes over time. An important goal is to determine the\r\nfixation
probability of a single advantageous mutant that arises in a homogeneous\r\npopulation
of N residents. Many real populations experience environmental\r\ngradients that
cause mutations to be beneficial in some spatial\r\nregions but harmful in others.
Here, we study the fixation probability of a\r\nmutant placed on a simple one-dimensional
spatial structure that experiences\r\nsuch a gradient. The mutant’s fitness varies
linearly from1 − s to 1 + s, whereas\r\nthe resident fitness is constant and equal
to 1. The existing literature suggests\r\nthat such heterogeneity in the mutant’s
fitness should lead to a decrease in its\r\nfixation probability. However, in
this work, we find that small, non-negligible\r\ngradients (s < 1=√N) substantially
increase the fixation probability,while larger\r\ngradients (s > (log N)/√N) substantially
decrease it.Moreover, we quantify the\r\nstrength of this phenomenon analytically
and we precisely delimit the range of\r\nthe gradients for which it occurs. Our
computer simulations closely match\r\nthose findings. Altogether, our results
indicate that subjecting a simple\r\npopulation structure to natural environmental
conditions can produce strong\r\ncounterintuitive effects."
acknowledgement: "J.S. and K.C. were supported by the European Research Council (ERC)\r\nCoG
863818 (ForM-SMArt) and Austrian Science Fund (FWF) 10.55776/\r\nCOE12. J.T. was
supported by GAČR grant 25-17377S and by Charles\r\nUniv. projects UNCE 24/SCI/008
and PRIMUS 24/SCI/012."
article_number: '5325'
article_processing_charge: Yes
article_type: original
author:
- first_name: Jakub
full_name: Svoboda, Jakub
id: 130759D2-D7DD-11E9-87D2-DE0DE6697425
last_name: Svoboda
orcid: 0000-0002-1419-3267
- first_name: Hossein
full_name: Nemati, Hossein
last_name: Nemati
- first_name: Josef
full_name: Tkadlec, Josef
id: 3F24CCC8-F248-11E8-B48F-1D18A9856A87
last_name: Tkadlec
orcid: 0000-0002-1097-9684
- first_name: Kamran
full_name: Kaveh, Kamran
last_name: Kaveh
- first_name: Krishnendu
full_name: Chatterjee, Krishnendu
id: 2E5DCA20-F248-11E8-B48F-1D18A9856A87
last_name: Chatterjee
orcid: 0000-0002-4561-241X
citation:
ama: Svoboda J, Nemati H, Tkadlec J, Kaveh K, Chatterjee K. The effect of the fitness
gradient on fixation probability. Nature Communications. 2026;17. doi:10.1038/s41467-026-71777-2
apa: Svoboda, J., Nemati, H., Tkadlec, J., Kaveh, K., & Chatterjee, K. (2026).
The effect of the fitness gradient on fixation probability. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-026-71777-2
chicago: Svoboda, Jakub, Hossein Nemati, Josef Tkadlec, Kamran Kaveh, and Krishnendu
Chatterjee. “The Effect of the Fitness Gradient on Fixation Probability.” Nature
Communications. Springer Nature, 2026. https://doi.org/10.1038/s41467-026-71777-2.
ieee: J. Svoboda, H. Nemati, J. Tkadlec, K. Kaveh, and K. Chatterjee, “The effect
of the fitness gradient on fixation probability,” Nature Communications,
vol. 17. Springer Nature, 2026.
ista: Svoboda J, Nemati H, Tkadlec J, Kaveh K, Chatterjee K. 2026. The effect of
the fitness gradient on fixation probability. Nature Communications. 17, 5325.
mla: Svoboda, Jakub, et al. “The Effect of the Fitness Gradient on Fixation Probability.”
Nature Communications, vol. 17, 5325, Springer Nature, 2026, doi:10.1038/s41467-026-71777-2.
short: J. Svoboda, H. Nemati, J. Tkadlec, K. Kaveh, K. Chatterjee, Nature Communications
17 (2026).
corr_author: '1'
das_tickbox: '0'
dataavailabilitystatement: Correspondence and requests for materials should be addressed
to Krishnendu Chatterjee.
date_created: 2026-06-21T22:02:59Z
date_published: 2026-12-01T00:00:00Z
date_updated: 2026-06-24T07:53:53Z
day: '01'
ddc:
- '000'
department:
- _id: KrCh
doi: 10.1038/s41467-026-71777-2
ec_funded: 1
external_id:
pmid:
- '41997932'
file:
- access_level: open_access
checksum: b660048bb271f24d6763803e247d5c32
content_type: application/pdf
creator: dernst
date_created: 2026-06-24T06:50:24Z
date_updated: 2026-06-24T06:50:24Z
file_id: '22136'
file_name: 2026_NatureComm_Svoboda.pdf
file_size: 1068919
relation: main_file
success: 1
file_date_updated: 2026-06-24T06:50:24Z
has_accepted_license: '1'
intvolume: ' 17'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 0599E47C-7A3F-11EA-A408-12923DDC885E
call_identifier: H2020
grant_number: '863818'
name: 'Formal Methods for Stochastic Models: Algorithms and Applications'
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
researchdata_availability: no
scopus_import: '1'
status: public
supplementarymaterial: yes
title: The effect of the fitness gradient on fixation probability
tmp:
image: /images/cc_by_nc_nd.png
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: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2026'
...
---
OA_place: repository
OA_type: green
_id: '22103'
abstract:
- lang: eng
text: "Modern AI systems increasingly rely on opaque, highly complex models whose
inner workings remain inaccessible even to experts. This opacity creates challenges
for trust, accountability, and compliance with\r\nemerging regulatory expectations
such as the “right to an explanation”. While traditional explainability methods—feature
attributions, counterfactuals, surrogate models—and interpretable model classes
provide valuable insights for engineers, they often fall short of delivering the
contextual, conversational explanations that\r\nreal users expect. Large Language
Models (LLMs) offer a promising new avenue for explanation due to their\r\nability
to engage interactively, adapt to user needs, and translate technical outputs
into more accessible reasoning. However, their tendencies toward hallucination,
conflict avoidance, and oversimplification introduce\r\nserious risks when used
as explanatory agents. This paper analyzes these opportunities and limitations,
examines verification strategies for ensuring explanation fidelity, and situates
LLM-generated explanations within\r\nbroader concerns about public trust. The
paper concludes by outlining best practices and future research directions for
building robust, verifiable, and human-aligned explanation systems."
acknowledgement: "This work has been supported by the European Research Council under
Grant No.: ERC-2020-AdG\r\n101020093. LLM–based tools have been used as\r\nwriting
assistance to help improve presentation.\r\n"
article_processing_charge: No
author:
- first_name: Filip
full_name: Cano Cordoba, Filip
id: 708cad98-e86a-11ef-8098-bdae2d7c6af1
last_name: Cano Cordoba
orcid: 0000-0002-0783-904X
citation:
ama: 'Cano Cordoba F. Explaining decisions one conversation at a time: Opportunities
and risks of LLMs as explainability assistants. In: Proceedings of the 18th
International Conference on Agents and Artificial Intelligence. Vol 5. Science
and Technology Publications; 2026:4689-4696. doi:10.5220/0014483200004052'
apa: 'Cano Cordoba, F. (2026). Explaining decisions one conversation at a time:
Opportunities and risks of LLMs as explainability assistants. In Proceedings
of the 18th International Conference on Agents and Artificial Intelligence
(Vol. 5, pp. 4689–4696). Marbella, Spain: Science and Technology Publications.
https://doi.org/10.5220/0014483200004052'
chicago: 'Cano Cordoba, Filip. “Explaining Decisions One Conversation at a Time:
Opportunities and Risks of LLMs as Explainability Assistants.” In Proceedings
of the 18th International Conference on Agents and Artificial Intelligence,
5:4689–96. Science and Technology Publications, 2026. https://doi.org/10.5220/0014483200004052.'
ieee: 'F. Cano Cordoba, “Explaining decisions one conversation at a time: Opportunities
and risks of LLMs as explainability assistants,” in Proceedings of the 18th
International Conference on Agents and Artificial Intelligence, Marbella,
Spain, 2026, vol. 5, pp. 4689–4696.'
ista: 'Cano Cordoba F. 2026. Explaining decisions one conversation at a time: Opportunities
and risks of LLMs as explainability assistants. Proceedings of the 18th International
Conference on Agents and Artificial Intelligence. ICAART: International Conference
on Agents and Artificial Intelligence vol. 5, 4689–4696.'
mla: 'Cano Cordoba, Filip. “Explaining Decisions One Conversation at a Time: Opportunities
and Risks of LLMs as Explainability Assistants.” Proceedings of the 18th International
Conference on Agents and Artificial Intelligence, vol. 5, Science and Technology
Publications, 2026, pp. 4689–96, doi:10.5220/0014483200004052.'
short: F. Cano Cordoba, in:, Proceedings of the 18th International Conference on
Agents and Artificial Intelligence, Science and Technology Publications, 2026,
pp. 4689–4696.
conference:
end_date: 2026-03-08
location: Marbella, Spain
name: 'ICAART: International Conference on Agents and Artificial Intelligence'
start_date: 2026-03-05
corr_author: '1'
das_tickbox: '0'
date_created: 2026-06-21T22:03:00Z
date_published: 2026-04-01T00:00:00Z
date_updated: 2026-06-24T08:37:00Z
day: '01'
department:
- _id: ToHe
doi: 10.5220/0014483200004052
ec_funded: 1
intvolume: ' 5'
keyword:
- Explainable AI
- Large Language Models
- Trust in AI
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://filipcano.org/files/icaart26llm.pdf
month: '04'
oa: 1
oa_version: Accepted Version
page: 4689-4696
project:
- _id: 62781420-2b32-11ec-9570-8d9b63373d4d
call_identifier: H2020
grant_number: '101020093'
name: Vigilant Algorithmic Monitoring of Software
publication: Proceedings of the 18th International Conference on Agents and Artificial
Intelligence
publication_identifier:
eissn:
- 2184-433X
isbn:
- '9789897587962'
issn:
- 2184-3589
publication_status: published
publisher: Science and Technology Publications
quality_controlled: '1'
researchdata_availability: no
scopus_import: '1'
status: public
supplementarymaterial: no
title: 'Explaining decisions one conversation at a time: Opportunities and risks of
LLMs as explainability assistants'
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2026'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '22105'
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
license: https://creativecommons.org/licenses/by/4.0/
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:
record:
- id: '20641'
relation: research_data
status: public
- id: '21145'
relation: research_data
status: public
researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 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:
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first_name: Haohao
last_name: Fu
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first_name: Benjamin
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last_name: Tatman
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first_name: Matthias
last_name: Dreydoppel
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last_name: Kapitonova
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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:
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department:
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- _id: PaSc
doi: 10.15479/AT-ISTA-21145
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title: Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics
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