---
OA_place: repository
_id: '22687'
abstract:
- lang: eng
text: "Understanding enzyme function requires characterizing not only static structure
but also dynamics and ligand interactions. NMR spectroscopy provides this insight
at atomic resolution, yet for large proteins the difficulty of resonance assignment
has largely confined such studies to systems below ∼50 kDa, or to observing only
methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution
NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus
(IiMDH), an enzyme of particular interest as an evolutionary intermediate between
allosteric lactate\r\ndehydrogenases and non-allosteric malate dehydrogenases.
By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein
with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment
of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building
on these assignments, we use various probes of backbone and sidechain dynamics:
elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions
in functionally critical regions, including the catalytic loop and the mobile
surface loop. Complementary methyl-axis order parameters from solution NMR identified
additional flexible sites in the hydrophobic core. Chemical shift perturbation
experiments upon addition of the substrate analogue oxamate, monitored via backbone
1H-15N TROSY, revealed both active-site contacts and responses in helices α2F
and α3G, regions implicated in allosteric signal transmission. The integrated
approach demonstrated here exploits the distinct strengths of MAS and solution
NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions
in a large oligomeric enzyme that would not be accessible by either technique
alone."
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: This research was supported by the Scientific Service Units (SSU)
of Institute of Science and Technology Austria (ISTA) through resources provided
by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra
Rovó, Megha Mohan and Margarita Valhondo Falcón for excellent support of the NMR
facility.
article_processing_charge: No
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
citation:
ama: 'Schanda P, Napoli F. Data and scripts for: “Integrated solid/solution NMR
assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” 2026.
doi:10.15479/AT-ISTA-22687'
apa: 'Schanda, P., & Napoli, F. (2026). Data and scripts for: “Integrated solid/solution
NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.”
Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-22687'
chicago: 'Schanda, Paul, and Federico Napoli. “Data and Scripts for: ‘Integrated
Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a
134 KDa Enzyme.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-22687.'
ieee: 'P. Schanda and F. Napoli, “Data and scripts for: ‘Integrated solid/solution
NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.’”
Institute of Science and Technology Austria, 2026.'
ista: 'Schanda P, Napoli F. 2026. Data and scripts for: ‘Integrated solid/solution
NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme’,
Institute of Science and Technology Austria, 10.15479/AT-ISTA-22687.'
mla: 'Schanda, Paul, and Federico Napoli. Data and Scripts for: “Integrated Solid/Solution
NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.”
Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-22687.'
short: P. Schanda, F. Napoli, (2026).
contributor:
- contributor_type: researcher
first_name: Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- contributor_type: project_leader
first_name: Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- contributor_type: project_member
first_name: Rajkumar
id: a3089acd-6806-11ee-bacc-f0c7d500ad20
last_name: Singh
- contributor_type: project_member
first_name: Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- contributor_type: project_member
first_name: Virgil
last_name: Aitenbichler
- contributor_type: project_member
first_name: Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- contributor_type: data_collector
first_name: Barbara
last_name: Perrone
corr_author: '1'
date_created: 2026-08-12T16:12:19Z
date_published: 2026-08-20T00:00:00Z
date_updated: 2026-08-20T07:40:15Z
day: '20'
department:
- _id: PaSc
doi: 10.15479/AT-ISTA-22687
doi_confirm: '1'
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file_id: '22743'
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file_size: 868
relation: main_file
success: 1
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has_accepted_license: '1'
month: '08'
oa: 1
oa_version: None
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publisher: Institute of Science and Technology Austria
status: public
title: 'Data and scripts for: "Integrated solid/solution NMR assignment allows mapping
dynamics and ligand binding in a 134 kDa enzyme"'
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'
...
---
OA_place: publisher
OA_type: gold
_id: '21327'
abstract:
- lang: eng
text: Proteins exist as a dynamic ensemble of multiple conformations, and these
motions are often crucial for their functions. However, current structure prediction
methods predominantly yield a single conformation, overlooking the conformational
heterogeneity revealed by diverse experimental modalities. Here, we present a
framework for building experiment-grounded protein structure generative models
that infer conformational ensembles consistent with measured experimental data.
The key idea is to treat stateof-the-art protein structure predictors (e.g., AlphaFold3)
as sequence-conditioned structural priors, and cast ensemble modeling as posterior
inference of protein structures given experimental measurements. Through extensive
real-data experiments, we demonstrate the generality of our method to incorporate
a variety of experimental measurements. In particular, our framework uncovers
previously unmodeled conformational heterogeneity from crystallographic densities,
and generates high-accuracy NMR ensembles orders of magnitude faster than the
status quo. Notably, we demonstrate that our ensembles outperform AlphaFold3 (Abramson
et al., 2024) and sometimes better fit experimental data than publicly deposited
structures to the Protein Data Bank (PDB, Burley et al. (2017)). We believe that
this approach will unlock building predictive models that fully embrace experimentally
observed conformational diversity.
acknowledged_ssus:
- _id: ScienComp
acknowledgement: 'This work was supported by the Israeli Science Foundation (ISF)
grant number 1834/24. We acknowledge support from the Austrian Science Fund (FWF,
grant numbers I5812-B and I6223) and the financial support of the Helmsley Fellowships
Program for Sustainability and Health. This research uses resources of the Institute
of Science and Technology Austria’s scientific computing cluster. '
alternative_title:
- PMLR
article_processing_charge: No
arxiv: 1
author:
- first_name: Sai A
full_name: Maddipatla, Sai A
id: e957f5e5-91c9-11f0-a95f-e090f66ecb4d
last_name: Maddipatla
- first_name: Nadav E
full_name: Sellam, Nadav E
id: ef280fe0-91c9-11f0-a95f-8dea3f5bc513
last_name: Sellam
- first_name: Meital I
full_name: Bojan, Meital I
id: 11d88cf5-91ca-11f0-a95f-edf9f08f47b7
last_name: Bojan
- first_name: Sanketh
full_name: Vedula, Sanketh
id: 94f2fe44-70fa-11f0-b76b-92922c09452b
last_name: Vedula
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Ailie
full_name: Marx, Ailie
last_name: Marx
- first_name: Alexander
full_name: Bronstein, Alexander
id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6
last_name: Bronstein
orcid: 0000-0001-9699-8730
citation:
ama: 'Maddipatla SA, Sellam NE, Bojan MI, et al. Inverse problems with experiment-guided
AlphaFold. In: Proceedings of the 42nd International Conference on Machine
Learning. Vol 267. ML Research Press; 2025:42366-42393.'
apa: 'Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Vedula, S., Schanda, P., Marx,
A., & Bronstein, A. M. (2025). Inverse problems with experiment-guided AlphaFold.
In Proceedings of the 42nd International Conference on Machine Learning
(Vol. 267, pp. 42366–42393). Vancouver, Canada: ML Research Press.'
chicago: Maddipatla, Sai A, Nadav E Sellam, Meital I Bojan, Sanketh Vedula, Paul
Schanda, Ailie Marx, and Alex M. Bronstein. “Inverse Problems with Experiment-Guided
AlphaFold.” In Proceedings of the 42nd International Conference on Machine
Learning, 267:42366–93. ML Research Press, 2025.
ieee: S. A. Maddipatla et al., “Inverse problems with experiment-guided AlphaFold,”
in Proceedings of the 42nd International Conference on Machine Learning,
Vancouver, Canada, 2025, vol. 267, pp. 42366–42393.
ista: 'Maddipatla SA, Sellam NE, Bojan MI, Vedula S, Schanda P, Marx A, Bronstein
AM. 2025. Inverse problems with experiment-guided AlphaFold. Proceedings of the
42nd International Conference on Machine Learning. ICML: International Conference
on Machine Learning, PMLR, vol. 267, 42366–42393.'
mla: Maddipatla, Sai A., et al. “Inverse Problems with Experiment-Guided AlphaFold.”
Proceedings of the 42nd International Conference on Machine Learning, vol.
267, ML Research Press, 2025, pp. 42366–93.
short: S.A. Maddipatla, N.E. Sellam, M.I. Bojan, S. Vedula, P. Schanda, A. Marx,
A.M. Bronstein, in:, Proceedings of the 42nd International Conference on Machine
Learning, ML Research Press, 2025, pp. 42366–42393.
conference:
end_date: 2025-07-19
location: Vancouver, Canada
name: 'ICML: International Conference on Machine Learning'
start_date: 2025-07-13
corr_author: '1'
date_created: 2026-02-18T12:11:17Z
date_published: 2025-07-30T00:00:00Z
date_updated: 2026-02-19T08:56:43Z
day: '30'
ddc:
- '000'
- '540'
department:
- _id: PaSc
- _id: AlBr
- _id: GradSch
external_id:
arxiv:
- '2502.09372'
file:
- access_level: open_access
checksum: f33230a6d59b7978d4cd72795e4e9059
content_type: application/pdf
creator: dernst
date_created: 2026-02-19T08:56:10Z
date_updated: 2026-02-19T08:56:10Z
file_id: '21338'
file_name: 2025_ICML_Maddipatla.pdf
file_size: 1924177
relation: main_file
success: 1
file_date_updated: 2026-02-19T08:56:10Z
has_accepted_license: '1'
intvolume: ' 267'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 42366 - 42393
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
- _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0
grant_number: I06223
name: Structure and mechanism of the mitochondrial MIM insertase
publication: Proceedings of the 42nd International Conference on Machine Learning
publication_identifier:
eissn:
- 2640-3498
publication_status: published
publisher: ML Research Press
quality_controlled: '1'
status: public
title: Inverse problems with experiment-guided AlphaFold
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: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 267
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '19555'
abstract:
- lang: eng
text: The charged arginine side chain is unique in determining many innate properties
of proteins, contributing to stability and interaction surfaces, and directing
allosteric regulation and enzymatic catalysis. NMR experiments can be used to
reveal these processes at the molecular level, but it often requires selective
insertion of carbon-13, nitrogen-15, and deuterium at defined atomic positions.
We introduce a method to endow arginine residues with defined isotope patterns,
combining synthetic organic chemistry and cell-based protein overexpression. The
resulting proteins feature NMR active spin systems with optimized relaxation pathways
leading to simplified NMR spectra with a sensitive response to changes in the
chemical environment of the nuclei observed.
acknowledged_ssus:
- _id: NMR
acknowledgement: We thank Lea Marie Becker for assistance with python scripts used
to analyze the labeling efficiency, and Undina Guillerm, Rajkumar Singh, and Anna
Kapitonova for help with protein production. This work was supported by the Austrian
Science Fund (FWF; project number I5812-B) through a French-Austrian bi-national
research project. We thank the Scientific Service Units (SSU) of Institute of Science
and Technology Austria (ISTA) through resources provided by the NMR Facility, as
well as the NMR center and MS center of the University of Vienna.
article_number: e202500408
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Darja
full_name: Rohden, Darja
id: 81dc668a-19fa-11f0-bf31-d56534059ef3
last_name: Rohden
- first_name: Giorgia
full_name: Toscano, Giorgia
last_name: Toscano
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Roman J.
full_name: Lichtenecker, Roman J.
last_name: Lichtenecker
citation:
ama: Rohden D, Toscano G, Schanda P, Lichtenecker RJ. Synthesis of selectively 13C/2H/15N-
labeled arginine to probe protein conformation and interaction by NMR spectroscopy.
Chemistry - A European Journal. 2025;31(24). doi:10.1002/chem.202500408
apa: Rohden, D., Toscano, G., Schanda, P., & Lichtenecker, R. J. (2025). Synthesis
of selectively 13C/2H/15N- labeled arginine to probe protein conformation and
interaction by NMR spectroscopy. Chemistry - A European Journal. Wiley.
https://doi.org/10.1002/chem.202500408
chicago: Rohden, Darja, Giorgia Toscano, Paul Schanda, and Roman J. Lichtenecker.
“Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation
and Interaction by NMR Spectroscopy.” Chemistry - A European Journal. Wiley,
2025. https://doi.org/10.1002/chem.202500408.
ieee: D. Rohden, G. Toscano, P. Schanda, and R. J. Lichtenecker, “Synthesis of selectively
13C/2H/15N- labeled arginine to probe protein conformation and interaction by
NMR spectroscopy,” Chemistry - A European Journal, vol. 31, no. 24. Wiley,
2025.
ista: Rohden D, Toscano G, Schanda P, Lichtenecker RJ. 2025. Synthesis of selectively
13C/2H/15N- labeled arginine to probe protein conformation and interaction by
NMR spectroscopy. Chemistry - A European Journal. 31(24), e202500408.
mla: Rohden, Darja, et al. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine
to Probe Protein Conformation and Interaction by NMR Spectroscopy.” Chemistry
- A European Journal, vol. 31, no. 24, e202500408, Wiley, 2025, doi:10.1002/chem.202500408.
short: D. Rohden, G. Toscano, P. Schanda, R.J. Lichtenecker, Chemistry - A European
Journal 31 (2025).
corr_author: '1'
date_created: 2025-04-13T22:01:19Z
date_published: 2025-04-25T00:00:00Z
date_updated: 2025-09-30T11:35:05Z
day: '25'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1002/chem.202500408
external_id:
isi:
- '001479486400019'
pmid:
- '40080421'
file:
- access_level: open_access
checksum: e3788628644b5aac666cf079b05f8fa7
content_type: application/pdf
creator: dernst
date_created: 2025-08-05T12:59:24Z
date_updated: 2025-08-05T12:59:24Z
file_id: '20136'
file_name: 2025_ChemistryEur_Rohden.pdf
file_size: 2840681
relation: main_file
success: 1
file_date_updated: 2025-08-05T12:59:24Z
has_accepted_license: '1'
intvolume: ' 31'
isi: 1
issue: '24'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Chemistry - A European Journal
publication_identifier:
eissn:
- 1521-3765
issn:
- 0947-6539
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation
and interaction by NMR spectroscopy
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 31
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20538'
abstract:
- lang: eng
text: In this study, we describe an integrated approach for methyl group assignment
comprising precursor-based selective methyl group labeling, a novel pulse sequence
for methyl to backbone coherence transfer and chemical shift predictions using
UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the
adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal
methyl groups of leucine and valine residues to each other and to the protein
backbone. By additional 13C,2H-labeling of residues other than valine and leucine
residues of the protein, important chemical shift information about neighboring
residues (following valine and leucine residues) can be achieved. Thus, different
valine and leucine residues in a protein can be characterized as a specific chemical
shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0
using experimental data taken from a subset of the BMRB database revealed a correct
assignment performance of about 90%. With applications to proteins of 60.2 kDa
and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides
valuable information even for very large proteins.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral
School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B.
This work was supported financially by the Austrian Science Fund (FWF, grant numbers
I06223 and I5812-B, “AlloSpace”). This research was supported by the Scientific
Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through
resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support
Facility (LSF). We thank Celina Sailer for assistance with the analysis of the NMR
spectrum of HsTom70.
article_number: '169465'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Sonja
full_name: Knödlstorfer, Sonja
last_name: Knödlstorfer
- first_name: Giorgia
full_name: Toscano, Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- first_name: Aleksandra L.
full_name: Ptaszek, Aleksandra L.
last_name: Ptaszek
- first_name: Georg
full_name: Kontaxis, Georg
last_name: Kontaxis
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Jakob
full_name: Schneider, Jakob
id: 64368429-eb97-11eb-a6c2-c980b1f44415
last_name: Schneider
- first_name: Katharina
full_name: Maier, Katharina
last_name: Maier
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- 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
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
citation:
ama: Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy
for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with
UCBShift 2.0. Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169465
apa: Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider,
J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment
using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal
of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2025.169465
chicago: Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis,
Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC
NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate
Integrated with UCBShift 2.0.” Journal of Molecular Biology. Elsevier,
2025. https://doi.org/10.1016/j.jmb.2025.169465.
ieee: S. Knödlstorfer et al., “A novel HMBC-CC-HMQC NMR strategy for methyl
assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift
2.0,” Journal of Molecular Biology, vol. 437, no. 23. Elsevier, 2025.
ista: Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J,
Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC
NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate
integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465.
mla: Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment
Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” Journal
of Molecular Biology, vol. 437, no. 23, 169465, Elsevier, 2025, doi:10.1016/j.jmb.2025.169465.
short: S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider,
K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of
Molecular Biology 437 (2025).
date_created: 2025-10-26T23:01:35Z
date_published: 2025-12-01T00:00:00Z
date_updated: 2026-08-13T14:19:02Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.1016/j.jmb.2025.169465
external_id:
pmid:
- '41016549'
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month: '12'
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oa_version: Published Version
pmid: 1
project:
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grant_number: I06223
name: Structure and mechanism of the mitochondrial MIM insertase
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Journal of Molecular Biology
publication_identifier:
eissn:
- 1089-8638
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled
α-ketoisovalerate integrated with UCBShift 2.0
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 437
year: '2025'
...
---
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_id: '20258'
abstract:
- lang: eng
text: The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise
deuterated proteins holds great potential for high-resolution solution and magic-angle
spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues
play key roles for example at active sites of enzymes. Taking advantage of a chemically
synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we
demonstrate here the usefulness of proton-detected MAS NMR approaches to probe
arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric
enzyme malate dehydrogenase we detected a wide range of motions, from sites that
are rigid on time scales of at least tens of milliseconds to residues undergoing
predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements
enabled quantitative determination of these dynamics. We observed microsecond
dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to
sample different β-turn conformations on this time scale. The labeling scheme
and experiments presented here expand the toolkit for high-resolution proton-detected
MAS NMR.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: This work was supported financially by the Austrian Science Fund
(FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific
Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through
resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support
Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent
support of the NMR facility.
article_number: '169379'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Darja
full_name: Rohden, Darja
id: 81dc668a-19fa-11f0-bf31-d56534059ef3
last_name: Rohden
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Benjamin
full_name: Tatman, Benjamin
id: 71cda2f3-e604-11ee-a1df-da10587eda3f
last_name: Tatman
- first_name: Roman J.
full_name: Lichtenecker, Roman J.
last_name: Lichtenecker
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine
dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme.
Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169379
apa: Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &
Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with
a specific isotope-labeling scheme. Journal of Molecular Biology. Elsevier.
https://doi.org/10.1016/j.jmb.2025.169379
chicago: Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman
J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning
NMR with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology.
Elsevier, 2025. https://doi.org/10.1016/j.jmb.2025.169379.
ieee: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P.
Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific
isotope-labeling scheme,” Journal of Molecular Biology, vol. 437, no. 23.
Elsevier, 2025.
ista: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025.
Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
scheme. Journal of Molecular Biology. 437(23), 169379.
mla: Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR
with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology,
vol. 437, no. 23, 169379, Elsevier, 2025, doi:10.1016/j.jmb.2025.169379.
short: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda,
Journal of Molecular Biology 437 (2025).
corr_author: '1'
date_created: 2025-08-31T22:01:33Z
date_published: 2025-12-01T00:00:00Z
date_updated: 2026-08-13T14:19:01Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1016/j.jmb.2025.169379
external_id:
isi:
- '001618289100020'
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date_updated: 2025-12-29T14:51:40Z
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month: '12'
oa: 1
oa_version: Published Version
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Journal of Molecular Biology
publication_identifier:
eissn:
- 1089-8638
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '19956'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
scheme
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 437
year: '2025'
...
---
_id: '19956'
abstract:
- lang: eng
text: The specific introduction of 1H-13C or 1H-15N moieties into otherwise deuterated
proteins holds great potential for high-resolution solution and magic-angle spinning
(MAS) NMR studies of protein structure and dynamics. Arginine residues play key
roles for example at active sites of enzymes. Taking advantage of a chemically
synthesized Arg with a 13C-1H2 group in an otherwise deuterated backbone, we demonstrate
here the usefulness of proton-detected arginine MAS NMR approaches to probe arginine
dynamics. In experiments on crystalline ubiquitin and the 134 kDa tetrameric enzyme
malate dehydrogenase we detected a wide range of motions, from sites that are
rigid on time scales of at least tens of milliseconds to residues undergoing predominantly
nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled
quantitative determination of these dynamics. We observed microsecond dynamics
of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different
β-turn conformations on this time scale. The labeling scheme and experiments presented
here expand the toolkit for high-resolution proton-detected MAS NMR
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
article_processing_charge: No
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Schanda P. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific
Isotope-Labeling Scheme. 2025. doi:10.15479/AT-ISTA-19956
apa: Schanda, P. (2025). Arginine Dynamics Probed by Magic-Angle Spinning NMR with
a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria.
https://doi.org/10.15479/AT-ISTA-19956
chicago: Schanda, Paul. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with
a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria,
2025. https://doi.org/10.15479/AT-ISTA-19956.
ieee: P. Schanda, “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific
Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025.
ista: Schanda P. 2025. Arginine Dynamics Probed by Magic-Angle Spinning NMR with
a Specific Isotope-Labeling Scheme, Institute of Science and Technology Austria,
10.15479/AT-ISTA-19956.
mla: Schanda, Paul. Arginine Dynamics Probed by Magic-Angle Spinning NMR with
a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria,
2025, doi:10.15479/AT-ISTA-19956.
short: P. Schanda, (2025).
contributor:
- contributor_type: researcher
first_name: Darja
last_name: Rohden
- contributor_type: researcher
first_name: Federico
last_name: Napoli
- contributor_type: researcher
first_name: Ben
last_name: Tatman
- contributor_type: researcher
first_name: Paul
last_name: Schanda
corr_author: '1'
date_created: 2025-07-03T04:21:37Z
date_published: 2025-07-03T00:00:00Z
date_updated: 2026-08-13T14:19:01Z
day: '03'
ddc:
- '572'
department:
- _id: PaSc
doi: 10.15479/AT-ISTA-19956
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file_name: README
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date_created: 2025-07-03T10:30:55Z
date_updated: 2025-07-03T10:30:55Z
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date_created: 2025-08-14T07:06:58Z
date_updated: 2025-08-14T07:06:58Z
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has_accepted_license: '1'
month: '07'
oa: 1
oa_version: Published Version
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publisher: Institute of Science and Technology Austria
related_material:
record:
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relation: used_in_publication
status: public
status: public
title: Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling
Scheme
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: research_data
user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18910'
abstract:
- lang: eng
text: Proteins often undergo large-scale conformational transitions, in which secondary
and tertiary structure elements (loops, helices, and domains) change their structures
or their positions with respect to each other. Simple considerations suggest that
such dynamics should be relatively fast, but the functional cycles of many proteins
are often relatively slow. Sophisticated experimental methods are starting to
tackle this dichotomy and shed light on the contribution of large-scale conformational
dynamics to protein function. In this review, we focus on the contribution of
single-molecule Förster resonance energy transfer and nuclear magnetic resonance
(NMR) spectroscopies to the study of conformational dynamics. We briefly describe
the state of the art in each of these techniques and then point out their similarities
and differences, as well as the relative strengths and weaknesses of each. Several
case studies, in which the connection between fast conformational dynamics and
slower function has been demonstrated, are then introduced and discussed. These
examples include both enzymes and large protein machines, some of which have been
studied by both NMR and fluorescence spectroscopies.
acknowledgement: G.H. is the incumbent of the Hilda Pomeraniec Memorial Professorial
Chair. He has been partially funded by the European Research Council under the European
Union's Horizon 2020 research and innovation program (grant 742637, SMALLOSTERY),
by National Science Foundation–US-Israel Binational Science Foundation grant 2021700,
and by an Israel Science Foundation Breakthrough grant (1924/22). P.S. acknowledges
funding from the Austrian Science Fund (project “AlloSpace,” I05812) and intramural
funding from the Institute of Science and Technology Austria.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Gilad
full_name: Haran, Gilad
last_name: Haran
citation:
ama: Schanda P, Haran G. NMR and single-molecule FRET insights into fast protein
motions and their relation to function. Annual Review of Biophysics. 2024;53:247-273.
doi:10.1146/annurev-biophys-070323-022428
apa: Schanda, P., & Haran, G. (2024). NMR and single-molecule FRET insights
into fast protein motions and their relation to function. Annual Review of
Biophysics. Annual Reviews. https://doi.org/10.1146/annurev-biophys-070323-022428
chicago: Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights
into Fast Protein Motions and Their Relation to Function.” Annual Review of
Biophysics. Annual Reviews, 2024. https://doi.org/10.1146/annurev-biophys-070323-022428.
ieee: P. Schanda and G. Haran, “NMR and single-molecule FRET insights into fast
protein motions and their relation to function,” Annual Review of Biophysics,
vol. 53. Annual Reviews, pp. 247–273, 2024.
ista: Schanda P, Haran G. 2024. NMR and single-molecule FRET insights into fast
protein motions and their relation to function. Annual Review of Biophysics. 53,
247–273.
mla: Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into
Fast Protein Motions and Their Relation to Function.” Annual Review of Biophysics,
vol. 53, Annual Reviews, 2024, pp. 247–73, doi:10.1146/annurev-biophys-070323-022428.
short: P. Schanda, G. Haran, Annual Review of Biophysics 53 (2024) 247–273.
corr_author: '1'
date_created: 2025-01-27T13:40:34Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2025-09-09T12:06:24Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1146/annurev-biophys-070323-022428
external_id:
isi:
- '001278237500012'
pmid:
- '38346243'
file:
- access_level: open_access
checksum: c90861542ae3f9147939030d5bafed3c
content_type: application/pdf
creator: dernst
date_created: 2025-01-27T13:44:59Z
date_updated: 2025-01-27T13:44:59Z
file_id: '18911'
file_name: 2024_AnnualReviews_Schanda.pdf
file_size: 3025589
relation: main_file
success: 1
file_date_updated: 2025-01-27T13:44:59Z
has_accepted_license: '1'
intvolume: ' 53'
isi: 1
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 247-273
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Annual Review of Biophysics
publication_identifier:
eissn:
- 1936-1238
issn:
- 1936-122X
publication_status: published
publisher: Annual Reviews
quality_controlled: '1'
scopus_import: '1'
status: public
title: NMR and single-molecule FRET insights into fast protein motions and their relation
to function
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 53
year: '2024'
...
---
APC_amount: 1530 EUR
OA_place: publisher
OA_type: gold
_id: '15401'
abstract:
- lang: eng
text: Amide-proton-detected magic-angle-spinning NMR of deuterated proteins has
become a main technique in NMR-based structural biology. In standard deuteration
protocols that rely on D2O-based culture media, non-exchangeable amide sites remain
deuterated, making these sites unobservable. Here we demonstrate that proteins
produced with a H2O-based culture medium doped with deuterated cell lysate allow
scientists to overcome this “reprotonation bottleneck” while retaining a high
level of deuteration (ca. 80 %) and narrow linewidths. We quantified coherence
lifetimes of several proteins prepared with this labeling pattern over a range
of magic-angle-spinning (MAS) frequencies (40–100 kHz). We demonstrate that under
commonly used conditions (50–60 kHz MAS), the amide 1H linewidths with our labeling
approach are comparable to those of perdeuterated proteins and better than those
of protonated samples at 100 kHz. For three proteins in the 33–50 kDa size range,
many previously unobserved amides become visible. We report how to prepare the
deuterated cell lysate for our approach from fractions of perdeuterated cultures
which are usually discarded, and we show that such media can be used identically
to commercial media. The residual protonation of Hα sites allows for well-resolved
Hα-detected spectra and Hα resonance assignment, exemplified by the de novo assignment
of 168 Hα sites in a 39 kDa protein. The approach based on this H2O/cell-lysate
deuteration and MAS frequencies compatible with 1.3 or 1.9 mm rotors presents
a strong sensitivity benefit over 0.7 mm 100 kHz MAS experiments.
acknowledged_ssus:
- _id: NMR
acknowledgement: "We thank Dominique Madern (IBS Grenoble) for providing the plasmid
for MalDH and feedback on the article, Alicia Vallet for excellent support at the
Grenoble NMR facility, and Petra Rovo and Margarita Valhondo at the IST Austria
NMR Service Unit. We thank Dorothea Anrather in the mass spectrometry facility of
Max Perutz Labs for the mass spectrometry analysis using the instruments of the
Vienna BioCenter Core Facilities (VBCF). We are grateful to Jean-Pierre Andrieu
(Plateforme Seq3A, IBS Grenoble) for the analysis of the amino acid composition
of the in-house-prepared lysates. We are grateful to Rasmus Linser (Technical University
Dortmund) for sharing a paper draft describing a similar study. This work was supported
by the Austrian Science Fund (FWF; project number I5812-B). We thank Tobias Schubeis
(Lyon) and the reviewers for constructive input.\r\nThis research has been supported
by the Austrian Science Fund (grant no. I5812-B). Part of this work used the platforms
of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the
Grenoble Partnership for 40 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). IBS acknowledges integration
into the Interdisciplinary Research Institute of Grenoble (IRIG, 45 CEA). Charles-Adrien
Arnaud was funded by GRAL."
article_processing_charge: Yes
article_type: original
author:
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Jia-Ying
full_name: Guan, Jia-Ying
last_name: Guan
- first_name: Charles-Adrien
full_name: Arnaud, Charles-Adrien
last_name: Arnaud
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Cécile
full_name: Breyton, Cécile
last_name: Breyton
- 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, Guan J-Y, Arnaud C-A, et al. Deuteration of proteins boosted by
cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without
the reprotonation bottleneck. Magnetic Resonance. 2024;5(1):33-49. doi:10.5194/mr-5-33-2024'
apa: 'Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C.,
& Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution
amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck.
Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-5-33-2024'
chicago: 'Napoli, Federico, Jia-Ying Guan, Charles-Adrien Arnaud, Pavel Macek, Hugo
Fraga, Cécile Breyton, and Paul Schanda. “Deuteration of Proteins Boosted by Cell
Lysates: High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the
Reprotonation Bottleneck.” Magnetic Resonance. Copernicus Publications,
2024. https://doi.org/10.5194/mr-5-33-2024.'
ieee: 'F. Napoli et al., “Deuteration of proteins boosted by cell lysates:
High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation
bottleneck,” Magnetic Resonance, vol. 5, no. 1. Copernicus Publications,
pp. 33–49, 2024.'
ista: 'Napoli F, Guan J-Y, Arnaud C-A, Macek P, Fraga H, Breyton C, Schanda P. 2024.
Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha
magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic
Resonance. 5(1), 33–49.'
mla: 'Napoli, Federico, et al. “Deuteration of Proteins Boosted by Cell Lysates:
High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the Reprotonation
Bottleneck.” Magnetic Resonance, vol. 5, no. 1, Copernicus Publications,
2024, pp. 33–49, doi:10.5194/mr-5-33-2024.'
short: F. Napoli, J.-Y. Guan, C.-A. Arnaud, P. Macek, H. Fraga, C. Breyton, P. Schanda,
Magnetic Resonance 5 (2024) 33–49.
corr_author: '1'
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publication_identifier:
issn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
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title: 'Deuteration of proteins boosted by cell lysates: High-resolution amide and
Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck'
tmp:
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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
day: '01'
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- '570'
department:
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grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Current Opinion in Structural Biology
publication_identifier:
eissn:
- 1879-033X
issn:
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publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 82
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...