---
_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
doi: 10.15479/AT-ISTA-20641
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month: '11'
oa: 1
oa_version: Published Version
project:
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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
title: Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals
and Complexes"
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: research_data
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...
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OA_place: publisher
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_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'
file:
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date_created: 2025-12-30T10:29:08Z
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issue: '23'
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month: '12'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0
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'
...
---
OA_place: publisher
OA_type: hybrid
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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
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date_updated: 2026-08-13T14:19:01Z
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title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
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legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
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---
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abstract:
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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:
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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
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department:
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date_created: 2025-08-14T07:06:58Z
date_updated: 2025-08-14T07:06:58Z
file_id: '20172'
file_name: 20240903_ubi_DN_Argd1C13_2D_spectra.tar.xz
file_size: 4766564
relation: main_file
success: 1
file_date_updated: 2025-08-14T07:06:58Z
fulldoi: https://doi.org/10.15479/AT-ISTA-19956
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:
- id: '20258'
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'
...
---
_id: '17042'
abstract:
- lang: eng
text: 'Bacterial cell walls are gigadalton-large cross-linked polymers with a wide
range of motional amplitudes, including rather rigid as well as highly flexible
parts. Magic-angle spinning NMR is a powerful method to obtain atomic-level information
about intact cell walls. Here we investigate sensitivity and information content
of different homonuclear 13C-13C and heteronuclear H-N, H-C and N-C correlation
experiments. We demonstrate that a CPMAS CryoProbe yields ca. 8-fold increased
signal-to-noise over a room-temperature probe, or a ca. 3-4-fold larger per-mass
sensitivity. The increased sensitivity allowed to obtain high-resolution spectra
even on intact bacteria. Moreover, we compare resolution and sensitivity of 1H
MAS experiments obtained at 100 kHz vs. 55 kHz. Our study provides useful hints
for choosing experiments to extract atomic-level details on cell-wall samples. '
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. Raw data to “MAS NMR experiments of corynebacterial cell walls:
complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” 2024.
doi:10.15479/AT:ISTA:17042'
apa: 'Schanda, P. (2024). Raw data to “MAS NMR experiments of corynebacterial cell
walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.”
Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:17042'
chicago: 'Schanda, Paul. “Raw Data to ‘MAS NMR Experiments of Corynebacterial Cell
Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.’”
Institute of Science and Technology Austria, 2024. https://doi.org/10.15479/AT:ISTA:17042.'
ieee: 'P. Schanda, “Raw data to ‘MAS NMR experiments of corynebacterial cell walls:
complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.’” Institute
of Science and Technology Austria, 2024.'
ista: 'Schanda P. 2024. Raw data to ‘MAS NMR experiments of corynebacterial cell
walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments’,
Institute of Science and Technology Austria, 10.15479/AT:ISTA:17042.'
mla: 'Schanda, Paul. Raw Data to “MAS NMR Experiments of Corynebacterial Cell
Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.”
Institute of Science and Technology Austria, 2024, doi:10.15479/AT:ISTA:17042.'
short: P. Schanda, (2024).
contributor:
- contributor_type: data_collector
first_name: Alicia
last_name: Vallet
- contributor_type: data_collector
first_name: 'Isabel '
last_name: Ayala
- contributor_type: data_collector
first_name: Barbara
last_name: Perrone
- contributor_type: data_collector
first_name: Alia
last_name: Hassan
- contributor_type: data_collector
first_name: Catherine
last_name: Bougault
corr_author: '1'
date_created: 2024-05-22T12:04:54Z
date_published: 2024-05-22T00:00:00Z
date_updated: 2025-09-09T12:01:41Z
day: '22'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.15479/AT:ISTA:17042
file:
- access_level: open_access
checksum: eb55f0988342d927702353b75e07edfa
content_type: text/plain
creator: pschanda
date_created: 2024-05-22T12:05:13Z
date_updated: 2024-05-22T12:05:13Z
file_id: '17043'
file_name: Read_me.txt
file_size: 2132
relation: main_file
success: 1
- access_level: open_access
checksum: 3393592acaf5ee1e032052c236780914
content_type: application/zip
creator: pschanda
date_created: 2024-05-22T12:17:10Z
date_updated: 2024-05-22T12:17:10Z
file_id: '17044'
file_name: raw_data_CryoMAS_cyronebacteria.zip
file_size: 755704888
relation: main_file
success: 1
file_date_updated: 2024-05-22T12:17:10Z
fulldoi: https://doi.org/10.15479/AT:ISTA:17042
has_accepted_license: '1'
keyword:
- nuclear magnetic resonance
- NMR
- cellwall
- structural biology
- spectroscopy
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '05'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '17291'
relation: used_in_publication
status: public
status: public
title: 'Raw data to "MAS NMR experiments of corynebacterial cell walls: complementary
1H- and CPMAS CryoProbe-enhanced 13C-detected experiments"'
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: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '17291'
abstract:
- lang: eng
text: Bacterial cell walls are gigadalton-large cross-linked polymers with a wide
range of motional amplitudes, including rather rigid as well as highly flexible
parts. Magic-angle spinning NMR is a powerful method to obtain atomic-level information
about intact cell walls. Here we investigate sensitivity and information content
of different homonuclear 13Csingle bond13C and heteronuclear 1Hsingle bond15N,
1Hsingle bond13C and 15Nsingle bond13C correlation experiments. We demonstrate
that a CPMAS CryoProbe yields ca. 8-fold increased signal-to-noise over a room-temperature
probe, or a ca. 3–4-fold larger per-mass sensitivity. The increased sensitivity
allowed to obtain high-resolution spectra even on intact bacteria. Moreover, we
compare resolution and sensitivity of 1H MAS experiments obtained at 100 kHz vs.
55 kHz. Our study provides useful hints for choosing experiments to extract atomic-level
details on cell-wall samples.
acknowledgement: "This research was supported by the French Agence Nationale de la
Recherche (\r\nANR-16-CE11-0030-12, TransPepNMR). This work used the platforms of
the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the
Grenoble Partnership for Structural Biology (PSB), supported by FRISBI, France (ANR-10-INBS-0005-02\r\n)
and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles
Universitaires de Recherche), CBH-EUR-GS (ANR-17-EURE-0003). Financial support from
the IR INFRANALYTICS FR2054 for conducting the research and intramural funding by
the Institute of Science and Technology Austria (ISTA) are gratefully acknowledged."
article_number: '107708'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Barbara
full_name: Perrone, Barbara
last_name: Perrone
- first_name: Alia
full_name: Hassan, Alia
last_name: Hassan
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
- first_name: Catherine
full_name: Bougault, Catherine
last_name: Bougault
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Vallet A, Ayala I, Perrone B, et al. MAS NMR experiments of corynebacterial
cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.
Journal of Magnetic Resonance. 2024;364. doi:10.1016/j.jmr.2024.107708'
apa: 'Vallet, A., Ayala, I., Perrone, B., Hassan, A., Simorre, J.-P., Bougault,
C., & Schanda, P. (2024). MAS NMR experiments of corynebacterial cell walls:
Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments. Journal
of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2024.107708'
chicago: 'Vallet, Alicia, Isabel Ayala, Barbara Perrone, Alia Hassan, Jean-Pierre
Simorre, Catherine Bougault, and Paul Schanda. “MAS NMR Experiments of Corynebacterial
Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.”
Journal of Magnetic Resonance. Elsevier, 2024. https://doi.org/10.1016/j.jmr.2024.107708.'
ieee: 'A. Vallet et al., “MAS NMR experiments of corynebacterial cell walls:
Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments,” Journal
of Magnetic Resonance, vol. 364. Elsevier, 2024.'
ista: 'Vallet A, Ayala I, Perrone B, Hassan A, Simorre J-P, Bougault C, Schanda
P. 2024. MAS NMR experiments of corynebacterial cell walls: Complementary 1H-
and CPMAS CryoProbe-enhanced 13C-detected experiments. Journal of Magnetic Resonance.
364, 107708.'
mla: 'Vallet, Alicia, et al. “MAS NMR Experiments of Corynebacterial Cell Walls:
Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.” Journal
of Magnetic Resonance, vol. 364, 107708, Elsevier, 2024, doi:10.1016/j.jmr.2024.107708.'
short: A. Vallet, I. Ayala, B. Perrone, A. Hassan, J.-P. Simorre, C. Bougault, P.
Schanda, Journal of Magnetic Resonance 364 (2024).
corr_author: '1'
date_created: 2024-07-22T07:44:10Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2025-09-09T12:01:41Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.jmr.2024.107708
external_id:
isi:
- '001259302800001'
pmid:
- '38901173'
file:
- access_level: open_access
checksum: 4b59f4f0c287ecbafd808da1212ced38
content_type: application/pdf
creator: dernst
date_created: 2024-07-23T06:23:51Z
date_updated: 2024-07-23T06:23:51Z
file_id: '17316'
file_name: 2024_JourMagneticResonance_Vallet.pdf
file_size: 2236665
relation: main_file
success: 1
file_date_updated: 2024-07-23T06:23:51Z
fulldoi: https://doi.org/10.1016/j.jmr.2024.107708
has_accepted_license: '1'
intvolume: ' 364'
isi: 1
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '17042'
relation: research_data
status: public
scopus_import: '1'
status: public
title: 'MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS
CryoProbe-enhanced 13C-detected experiments'
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: 364
year: '2024'
...
---
OA_type: closed access
_id: '18167'
abstract:
- lang: eng
text: 'Holdase chaperones are essential in the mitochondrial membrane-protein biogenesis
as they stabilize preproteins and keep them in an import-competent state as they
travel through the aqueous cytosol and intermembrane space. The small TIM chaperones
of the mitochondrial intermembrane space function within a fine balance of client
promiscuity and high affinity binding, while being also able to release their
client proteins without significant energy barrier to the downstream insertases/translocases.
The tendency of the preproteins to aggregate and the dynamic nature of the preprotein—chaperone
complexes makes the preparation of these complexes challenging. Here we present
two optimized methods for complex formation of highly hydrophobic precursor proteins
and chaperones: a pull-down approach and an in-vitro translation strategy. In
the former, attaching the client protein to an affinity resin keeps the individual
client protein copies apart from each other and decreases the client self-aggregation
probability, thereby favouring complex formation. In the latter approach, a purified
chaperone, added to the cell-free protein synthesis, captures the nascent precursor
protein. The choice of method will depend on the desired client-chaperone complex
amount, or the need for specific labeling scheme.'
article_processing_charge: No
author:
- first_name: Undina
full_name: Guillerm, Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- first_name: Iva
full_name: Sučec, Iva
last_name: Sučec
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Guillerm U, Sučec I, Schanda P. Generation of TIM chaperone substrate complexes.
In: Methods in Enzymology. Vol 707. Elsevier; 2024:391-422. doi:10.1016/bs.mie.2024.07.051'
apa: Guillerm, U., Sučec, I., & Schanda, P. (2024). Generation of TIM chaperone
substrate complexes. In Methods in Enzymology (Vol. 707, pp. 391–422).
Elsevier. https://doi.org/10.1016/bs.mie.2024.07.051
chicago: Guillerm, Undina, Iva Sučec, and Paul Schanda. “Generation of TIM Chaperone
Substrate Complexes.” In Methods in Enzymology, 707:391–422. Elsevier,
2024. https://doi.org/10.1016/bs.mie.2024.07.051.
ieee: U. Guillerm, I. Sučec, and P. Schanda, “Generation of TIM chaperone substrate
complexes,” in Methods in Enzymology, vol. 707, Elsevier, 2024, pp. 391–422.
ista: 'Guillerm U, Sučec I, Schanda P. 2024.Generation of TIM chaperone substrate
complexes. In: Methods in Enzymology. vol. 707, 391–422.'
mla: Guillerm, Undina, et al. “Generation of TIM Chaperone Substrate Complexes.”
Methods in Enzymology, vol. 707, Elsevier, 2024, pp. 391–422, doi:10.1016/bs.mie.2024.07.051.
short: U. Guillerm, I. Sučec, P. Schanda, in:, Methods in Enzymology, Elsevier,
2024, pp. 391–422.
corr_author: '1'
date_created: 2024-10-01T10:58:27Z
date_published: 2024-09-13T00:00:00Z
date_updated: 2025-10-22T06:40:54Z
day: '13'
department:
- _id: PaSc
doi: 10.1016/bs.mie.2024.07.051
external_id:
pmid:
- '39488384'
fulldoi: https://doi.org/10.1016/bs.mie.2024.07.051
intvolume: ' 707'
language:
- iso: eng
month: '09'
oa_version: None
page: 391-422
pmid: 1
publication: Methods in Enzymology
publication_identifier:
issn:
- 0076-6879
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Generation of TIM chaperone substrate complexes
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 707
year: '2024'
...
---
_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
external_id:
pmid:
- '40384772'
file:
- access_level: open_access
checksum: d01074f6919387fcaf8c9ebed320ccae
content_type: application/pdf
creator: dernst
date_created: 2024-06-27T06:42:55Z
date_updated: 2024-06-27T06:42:55Z
file_id: '17181'
file_name: 2024_MagneticResonance_Aebischer.pdf
file_size: 6736194
relation: main_file
success: 1
file_date_updated: 2024-06-27T06:42:55Z
fulldoi: https://doi.org/10.5194/mr-5-69-2024
has_accepted_license: '1'
intvolume: ' 5'
issue: '1'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: 69-86
pmid: 1
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publication: Magnetic Resonance
publication_identifier:
eissn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
related_material:
record:
- id: '22906'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Evaluating the motional timescales contributing to averaged anisotropic interactions
in MAS solid-state NMR
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2024'
...
---
OA_place: repository
OA_type: green
_id: '22906'
article_processing_charge: No
author:
- first_name: Kathrin
full_name: Aebischer, Kathrin
last_name: Aebischer
citation:
ama: Aebischer K. Evaluating the motional time scales contributing to averaged anisotropic
interactions in MAS solid-state NMR. 2024. doi:10.3929/ethz-b-000666765
apa: Aebischer, K. (2024). Evaluating the motional time scales contributing to averaged
anisotropic interactions in MAS solid-state NMR. Repository. https://doi.org/10.3929/ethz-b-000666765
chicago: Aebischer, Kathrin. “Evaluating the Motional Time Scales Contributing to
Averaged Anisotropic Interactions in MAS Solid-State NMR.” Repository, 2024. https://doi.org/10.3929/ethz-b-000666765.
ieee: K. Aebischer, “Evaluating the motional time scales contributing to averaged
anisotropic interactions in MAS solid-state NMR.” Repository, 2024.
ista: Aebischer K. 2024. Evaluating the motional time scales contributing to averaged
anisotropic interactions in MAS solid-state NMR, Repository, 10.3929/ethz-b-000666765.
mla: Aebischer, Kathrin. Evaluating the Motional Time Scales Contributing to
Averaged Anisotropic Interactions in MAS Solid-State NMR. Repository, 2024,
doi:10.3929/ethz-b-000666765.
short: K. Aebischer, (2024).
contributor:
- contributor_type: contact_person
first_name: Matthias
last_name: Ernst
- contributor_type: data_collector
first_name: Kathrin
last_name: Aebischer
- contributor_type: data_collector
first_name: Matthias
last_name: Ernst
- contributor_type: data_collector
first_name: Paul
last_name: Schanda
- contributor_type: data_collector
first_name: Lea Marie
last_name: Becker
- contributor_type: producer
first_name: Matthias
last_name: ' Ernst'
- contributor_type: producer
first_name: Kathrin
last_name: ' Aebischer'
- contributor_type: producer
first_name: 'Paul '
last_name: Schanda
- contributor_type: producer
first_name: Lea Marie
last_name: Becker
date_created: 2026-09-11T08:49:48Z
date_published: 2024-04-03T00:00:00Z
date_updated: 2026-09-11T08:49:55Z
day: '03'
ddc:
- '530'
department:
- _id: PaSc
doi: 10.3929/ethz-b-000666765
fulldoi: https://doi.org/10.3929/ethz-b-000666765
main_file_link:
- open_access: '1'
url: https://doi.org/10.3929/ethz-b-000666765
month: '04'
oa: 1
oa_version: None
publisher: Repository
related_material:
record:
- id: '17161'
relation: used_in_publication
status: public
status: public
title: Evaluating the motional time scales contributing to averaged anisotropic interactions
in MAS solid-state NMR
type: research_data_reference
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
year: '2024'
...
---
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'
das_tickbox: '0'
date_created: 2025-01-27T13:40:34Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2026-09-17T09:44:33Z
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
fulldoi: https://doi.org/10.1146/annurev-biophys-070323-022428
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'
researchdata_availability: no
scopus_import: '1'
status: public
supplementarymaterial: no
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'
date_created: 2024-05-16T15:02:43Z
date_published: 2024-04-19T00:00:00Z
date_updated: 2026-09-24T10:36:36Z
day: '19'
ddc:
- '530'
department:
- _id: PaSc
doi: 10.5194/mr-5-33-2024
external_id:
pmid:
- '40384771'
file:
- access_level: open_access
checksum: 80ea50114e428461ca9530d3bd5d89e4
content_type: application/pdf
creator: dernst
date_created: 2024-05-22T07:01:15Z
date_updated: 2024-05-22T07:01:15Z
file_id: '15413'
file_name: 2024_MagneticResonance_Napoli.pdf
file_size: 6657865
relation: main_file
success: 1
file_date_updated: 2024-05-22T07:01:15Z
fulldoi: https://doi.org/10.5194/mr-5-33-2024
has_accepted_license: '1'
intvolume: ' 5'
issue: '1'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 33-49
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
- _id: 3AC91DDA-15DF-11EA-824D-93A3E7B544D1
call_identifier: FWF
name: FWF Open Access Fund
publication: Magnetic Resonance
publication_identifier:
issn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
related_material:
record:
- id: '22940'
relation: research_data
status: public
scopus_import: '1'
status: public
title: 'Deuteration of proteins boosted by cell lysates: High-resolution amide and
Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck'
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2024'
...
---
OA_place: repository
OA_type: green
_id: '22940'
article_processing_charge: No
author:
- first_name: Astrid
full_name: ' Sivertsen, Astrid'
last_name: ' Sivertsen'
- first_name: Federico
full_name: Napoli, Federico
last_name: Napoli
- first_name: Paul
full_name: Schanda, Paul
last_name: Schanda
citation:
ama: Sivertsen A, Napoli F, Schanda P. Amide and a-hydrogens extension to the Solid-state
NMR assignment of P. horikoshii TET2. 2024. doi:10.13018/BMR52400
apa: Sivertsen, A., Napoli, F., & Schanda, P. (2024). Amide and a-hydrogens
extension to the Solid-state NMR assignment of P. horikoshii TET2. Repository.
https://doi.org/10.13018/BMR52400
chicago: Sivertsen, Astrid, Federico Napoli, and Paul Schanda. “Amide and A-Hydrogens
Extension to the Solid-State NMR Assignment of P. Horikoshii TET2.” Repository,
2024. https://doi.org/10.13018/BMR52400.
ieee: A. Sivertsen, F. Napoli, and P. Schanda, “Amide and a-hydrogens extension
to the Solid-state NMR assignment of P. horikoshii TET2.” Repository, 2024.
ista: Sivertsen A, Napoli F, Schanda P. 2024. Amide and a-hydrogens extension to
the Solid-state NMR assignment of P. horikoshii TET2, Repository, 10.13018/BMR52400.
mla: Sivertsen, Astrid, et al. Amide and A-Hydrogens Extension to the Solid-State
NMR Assignment of P. Horikoshii TET2. Repository, 2024, doi:10.13018/BMR52400.
short: A. Sivertsen, F. Napoli, P. Schanda, (2024).
date_created: 2026-09-17T09:10:45Z
date_published: 2024-05-15T00:00:00Z
date_updated: 2026-09-24T10:36:36Z
day: '15'
ddc:
- '530'
department:
- _id: PaSc
doi: 10.13018/BMR52400
fulldoi: https://doi.org/10.13018/BMR52400
main_file_link:
- open_access: '1'
url: https://doi.org/10.13018/BMR52400
month: '05'
oa: 1
oa_version: None
publisher: Repository
related_material:
record:
- id: '15401'
relation: used_in_publication
status: public
status: public
title: Amide and a-hydrogens extension to the Solid-state NMR assignment of P. horikoshii
TET2
type: research_data_reference
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
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
- access_level: open_access
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: '12820'
abstract:
- lang: eng
text: "Disulfide bond formation is fundamentally important for protein structure,
and constitutes a key mechanism by which cells regulate the intracellular oxidation
state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen
peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally,
upon Cys oxidation PRDXs undergo extensive conformational rearrangements that
may underlie their presently structurally poorly defined functions as molecular
chaperones. Rearrangements include high molecular-weight oligomerization, the
dynamics of which are, however, poorly understood, as is the impact of disulfide
bond formation on these properties. Here we show that formation of disulfide bonds
along the catalytic cycle induces extensive microsecond time scale dynamics, as
monitored by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly
and solution-NMR of a designed dimeric mutant. We ascribe the conformational dynamics
to structural frustration, resulting from conflicts between the disulfide-constrained
reduction of mobility and the desire to fulfil other favorable contacts. \r\n\r\nThis
data repository contains NMR data presented in the associated manuscript"
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. Research data of the publication “Disulfide-bond-induced structural
frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” 2023. doi:10.15479/AT:ISTA:12820
apa: Schanda, P. (2023). Research data of the publication “Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.”
Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12820
chicago: Schanda, Paul. “Research Data of the Publication ‘Disulfide-Bond-Induced
Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.’”
Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:12820.
ieee: P. Schanda, “Research data of the publication ‘Disulfide-bond-induced structural
frustration and dynamic disorder in a peroxiredoxin from MAS NMR.’” Institute
of Science and Technology Austria, 2023.
ista: Schanda P. 2023. Research data of the publication ‘Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR’,
Institute of Science and Technology Austria, 10.15479/AT:ISTA:12820.
mla: Schanda, Paul. Research Data of the Publication “Disulfide-Bond-Induced
Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.”
Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12820.
short: P. Schanda, (2023).
contributor:
- contributor_type: researcher
first_name: Laura
last_name: Troussicot
- contributor_type: researcher
first_name: Björn M.
last_name: Burmann
corr_author: '1'
date_created: 2023-04-10T05:55:56Z
date_published: 2023-04-18T00:00:00Z
date_updated: 2024-10-09T21:05:30Z
day: '18'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.15479/AT:ISTA:12820
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date_updated: 2023-04-14T09:39:33Z
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date_created: 2023-04-14T09:39:58Z
date_updated: 2023-04-14T09:39:58Z
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file_name: README
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has_accepted_license: '1'
month: '04'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '13095'
relation: used_in_publication
status: public
status: public
title: Research data of the publication "Disulfide-bond-induced structural frustration
and dynamic disorder in a peroxiredoxin from MAS NMR"
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: '13095'
abstract:
- lang: eng
text: Disulfide bond formation is fundamentally important for protein structure
and constitutes a key mechanism by which cells regulate the intracellular oxidation
state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen
peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally,
upon Cys oxidation PRDXs undergo extensive conformational rearrangements that
may underlie their presently structurally poorly defined functions as molecular
chaperones. Rearrangements include high molecular-weight oligomerization, the
dynamics of which are, however, poorly understood, as is the impact of disulfide
bond formation on these properties. Here we show that formation of disulfide bonds
along the catalytic cycle induces extensive μs time scale dynamics, as monitored
by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly and solution-NMR
of a designed dimeric mutant. We ascribe the conformational dynamics to structural
frustration, resulting from conflicts between the disulfide-constrained reduction
of mobility and the desire to fulfill other favorable contacts.
acknowledgement: "We thank Albert A. Smith (Univ. Leipzig) for discussions and help
with detectors analyses, Undina Guillerm (IST Austria) for gel electrophoresis experiments
(Figure S7), and Jens\r\nLidman (Univ. Gothenburg) for a 3Q relaxation analysis
script. Intramural funding from Institute of Science and Technology Austria is acknowledged.
This work also used the platforms of\r\nthe Grenoble Instruct-ERIC center (ISBG;
UMS 3518 CNRSCEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology
(PSB), as well as the Swedish NMR Centre\r\nof the University of Gothenburg. Both
platforms provided excellent research infrastructures. B.M.B. gratefully acknowledges
funding from the Swedish Research Council (Starting grant 2016-04721), the Swedish
Cancer Foundation (2019-0415), and the Knut och Alice Wallenberg Foundation through
a Wallenberg Academy Fellowship (2016.0163) as well as through the Wallenberg Centre
for Molecular and Translational Medicine, University of Gothenburg, Sweden. "
article_processing_charge: No
article_type: original
author:
- first_name: Laura
full_name: Troussicot, Laura
id: 3d9cac31-413c-11eb-9514-d1ec2a7fb7f3
last_name: Troussicot
orcid: 0000-0001-8297-8886
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Mikael
full_name: Molin, Mikael
last_name: Molin
- first_name: Björn M.
full_name: Burmann, Björn M.
last_name: Burmann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal
of the American Chemical Society. 2023;145(19):10700–10711. doi:10.1021/jacs.3c01200
apa: Troussicot, L., Vallet, A., Molin, M., Burmann, B. M., & Schanda, P. (2023).
Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin
from MAS NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.3c01200
chicago: Troussicot, Laura, Alicia Vallet, Mikael Molin, Björn M. Burmann, and Paul
Schanda. “Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in
a Peroxiredoxin from MAS NMR.” Journal of the American Chemical Society.
American Chemical Society, 2023. https://doi.org/10.1021/jacs.3c01200.
ieee: L. Troussicot, A. Vallet, M. Molin, B. M. Burmann, and P. Schanda, “Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR,”
Journal of the American Chemical Society, vol. 145, no. 19. American Chemical
Society, pp. 10700–10711, 2023.
ista: Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. 2023. Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal
of the American Chemical Society. 145(19), 10700–10711.
mla: Troussicot, Laura, et al. “Disulfide-Bond-Induced Structural Frustration and
Dynamic Disorder in a Peroxiredoxin from MAS NMR.” Journal of the American
Chemical Society, vol. 145, no. 19, American Chemical Society, 2023, pp. 10700–10711,
doi:10.1021/jacs.3c01200.
short: L. Troussicot, A. Vallet, M. Molin, B.M. Burmann, P. Schanda, Journal of
the American Chemical Society 145 (2023) 10700–10711.
corr_author: '1'
date_created: 2023-05-28T22:01:04Z
date_published: 2023-05-04T00:00:00Z
date_updated: 2024-10-09T21:05:30Z
day: '04'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1021/jacs.3c01200
external_id:
isi:
- '000985907400001'
pmid:
- '37140345'
file:
- access_level: open_access
checksum: 0758a930ef21c62fc91b14e657479f83
content_type: application/pdf
creator: dernst
date_created: 2023-05-30T07:05:28Z
date_updated: 2023-05-30T07:05:28Z
file_id: '13098'
file_name: 2023_JACS_Troussicot.pdf
file_size: 6719299
relation: main_file
success: 1
file_date_updated: 2023-05-30T07:05:28Z
fulldoi: https://doi.org/10.1021/jacs.3c01200
has_accepted_license: '1'
intvolume: ' 145'
isi: 1
issue: '19'
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
page: 10700–10711
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
related_material:
record:
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relation: research_data
status: public
scopus_import: '1'
status: public
title: Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin
from MAS 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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 145
year: '2023'
...
---
_id: '13096'
abstract:
- lang: eng
text: Eukaryotic cells can undergo different forms of programmed cell death, many
of which culminate in plasma membrane rupture as the defining terminal event1,2,3,4,5,6,7.
Plasma membrane rupture was long thought to be driven by osmotic pressure, but
it has recently been shown to be in many cases an active process, mediated by
the protein ninjurin-18 (NINJ1). Here we resolve the structure of NINJ1 and the
mechanism by which it ruptures membranes. Super-resolution microscopy reveals
that NINJ1 clusters into structurally diverse assemblies in the membranes of dying
cells, in particular large, filamentous assemblies with branched morphology. A
cryo-electron microscopy structure of NINJ1 filaments shows a tightly packed fence-like
array of transmembrane α-helices. Filament directionality and stability is defined
by two amphipathic α-helices that interlink adjacent filament subunits. The NINJ1
filament features a hydrophilic side and a hydrophobic side, and molecular dynamics
simulations show that it can stably cap membrane edges. The function of the resulting
supramolecular arrangement was validated by site-directed mutagenesis. Our data
thus suggest that, during lytic cell death, the extracellular α-helices of NINJ1
insert into the plasma membrane to polymerize NINJ1 monomers into amphipathic
filaments that rupture the plasma membrane. The membrane protein NINJ1 is therefore
an interactive component of the eukaryotic cell membrane that functions as an
in-built breaking point in response to activation of cell death.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: "This work was supported by the Deutsche Forschungsgemeinschaft under
Germany’s Excellence Strategy EXC 2075–390740016 and the Stuttgart Center for Simulation
Science (SC SimTech) to K.P., by ERC-CoG 770988 (InflamCellDeath) and SNF Project
funding (310030B_198005, 310030B_192523) to P.B., by the Swiss Nanoscience Institute
and the Swiss National Science Foundation via the NCCR AntiResist (180541) to S.H.
and the NCCR Molecular Systems Engineering (51NF40-205608) to D.J.M., by the Helmholtz
Young Investigator Program of the Helmholtz Association to C.S., by the SNF Professorship
funding (PP00P3_198903) to C.P., EMBO postdoctoral fellowship ALTF 27-2022 to E.H.
and by the Scientific Service Units of IST Austria through resources provided by
the NMR and Life Science Facilities to P.S. Molecular dynamics simulations were
performed on the HoreKa supercomputer funded by the Ministry of Science, Research
and the Arts Baden-Württemberg and by the Federal Ministry of Education and Research.
The authors thank the BioEM Lab of the Biozentrum, University of Basel for support;
V. Mack, K. Shkarina and J. Fricke for technical support; D. Ricklin and S. Vogt
for peptide synthesis; P. Pelczar for support with animals; S.-J. Marrink and P.
Telles de Souza for supply with Martini3 parameters and scripts; and P. Radler und
M. Loose for help with QCM. Fig. 4g and Extended Data Fig. 1a were in part created
with BioRender.com.\r\nOpen access funding provided by University of Basel."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Morris
full_name: Degen, Morris
last_name: Degen
- first_name: José Carlos
full_name: Santos, José Carlos
last_name: Santos
- first_name: Kristyna
full_name: Pluhackova, Kristyna
last_name: Pluhackova
- first_name: Gonzalo
full_name: Cebrero, Gonzalo
last_name: Cebrero
- first_name: Saray
full_name: Ramos, Saray
last_name: Ramos
- first_name: Gytis
full_name: Jankevicius, Gytis
last_name: Jankevicius
- first_name: Ella
full_name: Hartenian, Ella
last_name: Hartenian
- first_name: Undina
full_name: Guillerm, Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- first_name: Stefania A.
full_name: Mari, Stefania A.
last_name: Mari
- first_name: Bastian
full_name: Kohl, Bastian
last_name: Kohl
- first_name: Daniel J.
full_name: Müller, Daniel J.
last_name: Müller
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Timm
full_name: Maier, Timm
last_name: Maier
- first_name: Camilo
full_name: Perez, Camilo
last_name: Perez
- first_name: Christian
full_name: Sieben, Christian
last_name: Sieben
- first_name: Petr
full_name: Broz, Petr
last_name: Broz
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
citation:
ama: Degen M, Santos JC, Pluhackova K, et al. Structural basis of NINJ1-mediated
plasma membrane rupture in cell death. Nature. 2023;618:1065-1071. doi:10.1038/s41586-023-05991-z
apa: Degen, M., Santos, J. C., Pluhackova, K., Cebrero, G., Ramos, S., Jankevicius,
G., … Hiller, S. (2023). Structural basis of NINJ1-mediated plasma membrane rupture
in cell death. Nature. Springer Nature. https://doi.org/10.1038/s41586-023-05991-z
chicago: Degen, Morris, José Carlos Santos, Kristyna Pluhackova, Gonzalo Cebrero,
Saray Ramos, Gytis Jankevicius, Ella Hartenian, et al. “Structural Basis of NINJ1-Mediated
Plasma Membrane Rupture in Cell Death.” Nature. Springer Nature, 2023.
https://doi.org/10.1038/s41586-023-05991-z.
ieee: M. Degen et al., “Structural basis of NINJ1-mediated plasma membrane
rupture in cell death,” Nature, vol. 618. Springer Nature, pp. 1065–1071,
2023.
ista: Degen M, Santos JC, Pluhackova K, Cebrero G, Ramos S, Jankevicius G, Hartenian
E, Guillerm U, Mari SA, Kohl B, Müller DJ, Schanda P, Maier T, Perez C, Sieben
C, Broz P, Hiller S. 2023. Structural basis of NINJ1-mediated plasma membrane
rupture in cell death. Nature. 618, 1065–1071.
mla: Degen, Morris, et al. “Structural Basis of NINJ1-Mediated Plasma Membrane Rupture
in Cell Death.” Nature, vol. 618, Springer Nature, 2023, pp. 1065–71, doi:10.1038/s41586-023-05991-z.
short: M. Degen, J.C. Santos, K. Pluhackova, G. Cebrero, S. Ramos, G. Jankevicius,
E. Hartenian, U. Guillerm, S.A. Mari, B. Kohl, D.J. Müller, P. Schanda, T. Maier,
C. Perez, C. Sieben, P. Broz, S. Hiller, Nature 618 (2023) 1065–1071.
date_created: 2023-05-28T22:01:04Z
date_published: 2023-06-29T00:00:00Z
date_updated: 2025-04-23T08:57:12Z
day: '29'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1038/s41586-023-05991-z
external_id:
isi:
- '000991386800011'
pmid:
- '37198476'
file:
- access_level: open_access
checksum: 0fab69252453bff1de7f0e2eceb76d34
content_type: application/pdf
creator: dernst
date_created: 2023-11-14T11:48:18Z
date_updated: 2023-11-14T11:48:18Z
file_id: '14533'
file_name: 2023_Nature_Degen.pdf
file_size: 12292188
relation: main_file
success: 1
file_date_updated: 2023-11-14T11:48:18Z
fulldoi: https://doi.org/10.1038/s41586-023-05991-z
has_accepted_license: '1'
intvolume: ' 618'
isi: 1
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: 1065-1071
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural basis of NINJ1-mediated plasma membrane rupture in cell death
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: 618
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: '14847'
abstract:
- lang: eng
text: Understanding the mechanisms of chaperones at the atomic level generally requires
producing chaperone–client complexes in vitro. This task comes with significant
challenges, because one needs to find conditions in which the client protein is
presented to the chaperone in a state that binds and at the same time avoid the
pitfalls of protein aggregation that are often inherent to such states. The strategy
differs significantly for different client proteins and chaperones, but there
are common underlying principles. Here, we discuss these principles and deduce
the strategies that can be successfully applied for different chaperone–client
complexes. We review successful biochemical strategies applied to making the client
protein “binding competent” and illustrate the different strategies with examples
of recent biophysical and biochemical studies.
alternative_title:
- New Developments in NMR
article_processing_charge: No
author:
- first_name: I.
full_name: Sučec, I.
last_name: Sučec
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical
and Structural Studies. In: Hiller S, Liu M, He L, eds. Biophysics of Molecular
Chaperones. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:10.1039/bk9781839165986-00136'
apa: Sučec, I., & Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies. In S. Hiller, M. Liu, & L. He (Eds.),
Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society
of Chemistry. https://doi.org/10.1039/bk9781839165986-00136
chicago: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” In Biophysics of Molecular Chaperones,
edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:136–61. Royal Society
of Chemistry, 2023. https://doi.org/10.1039/bk9781839165986-00136.
ieee: I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies,” in Biophysics of Molecular Chaperones,
vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023,
pp. 136–161.
ista: 'Sučec I, Schanda P. 2023.Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies. In: Biophysics of Molecular Chaperones. New
Developments in NMR, vol. 29, 136–161.'
mla: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” Biophysics of Molecular Chaperones,
edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023,
pp. 136–61, doi:10.1039/bk9781839165986-00136.
short: I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of
Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.
corr_author: '1'
date_created: 2024-01-22T08:04:57Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-10-09T21:07:57Z
day: '01'
department:
- _id: PaSc
doi: 10.1039/bk9781839165986-00136
editor:
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
- first_name: Maili
full_name: Liu, Maili
last_name: Liu
- first_name: Lichun
full_name: He, Lichun
last_name: He
fulldoi: https://doi.org/10.1039/bk9781839165986-00136
intvolume: ' 29'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.26434/chemrxiv-2023-rpn28
month: '11'
oa: 1
oa_version: Preprint
page: 136-161
publication: Biophysics of Molecular Chaperones
publication_identifier:
eisbn:
- '9781839165993'
isbn:
- '9781839162824'
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: Preparing Chaperone–Client Protein Complexes for Biophysical and Structural
Studies
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 29
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:
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fulldoi: https://doi.org/10.1002/anie.202219314
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issue: '19'
keyword:
- General Chemistry
- Catalysis
language:
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month: '05'
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publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
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issn:
- 1433-7851
publication_status: published
publisher: Wiley
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related_material:
link:
- description: News on ISTA website
relation: press_release
url: https://ista.ac.at/en/news/dancing-styles-of-atoms/
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title: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle
Spinning NMR of aromatic residues
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legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
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...