---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '21777'
abstract:
- lang: eng
text: The advantageous characteristics attributed to the 19F nucleus have made it
a popular target for nuclear magnetic resonance (NMR) once again in recent years.
Aside from solution NMR, an increasing number of studies have been conducted applying
solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here,
the high chemical shift anisotropy and strong dipolar couplings can be utilised
to get structural insights into proteins and measure long distances. Despite increasing
popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR
often suffers from slow longitudinal T1 relaxation and therefore long recycle
delays. In this work, we expand paramagnetic doping, an approach commonly used
to reduce proton T1 relaxation times, to 19F-labelled biological samples. We study
the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation
in a [5-19F13C]-tryptophan-labelled protein via 19F-detected MAS NMR experiments.
The observed paramagnetic relaxation enhancement substantially reduces measurement
times of 19F MAS NMR experiments without compromising resolution. Additionally,
we report the chemical shift assignments of all four fluorotryptophan signals
in the 12×39 kDa-large protein TET2 using a mutagenesis approach.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: We thank Ben P. Tatman for insightful discussions. This research
was supported by the Scientific Service Units (SSUs) of ISTA through resources provided
by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. We thank
Prof. Tobias Madl (Medical University Graz) for a sample of Omniscan. Lea M. Becker
is the recipient of a DOC fellowship of the Austrian Academy of Sciences at the
Institute of Science and Technology Austria (grant no. PR10660EAW01).
article_processing_charge: Yes
article_type: original
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Giorgia
full_name: Toscano, Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Rajkumar
full_name: Singh, Rajkumar
id: a3089acd-6806-11ee-bacc-f0c7d500ad20
last_name: Singh
- first_name: Undina
full_name: Guillerm, Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- first_name: Roman J.
full_name: Lichtenecker, Roman J.
last_name: Lichtenecker
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle
spinning NMR with paramagnetic dopants. Magnetic Resonance. 2026;7(1):29-37.
doi:10.5194/mr-7-29-2026
apa: Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker,
R. J., & Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning
NMR with paramagnetic dopants. Magnetic Resonance. Copernicus Publications.
https://doi.org/10.5194/mr-7-29-2026
chicago: Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina
Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular
Magic-Angle Spinning NMR with Paramagnetic Dopants.” Magnetic Resonance.
Copernicus Publications, 2026. https://doi.org/10.5194/mr-7-29-2026.
ieee: L. M. Becker et al., “Accelerated 19F biomolecular magic-angle spinning
NMR with paramagnetic dopants,” Magnetic Resonance, vol. 7, no. 1. Copernicus
Publications, pp. 29–37, 2026.
ista: Becker LM, Toscano G, Kapitonova A, Singh R, Guillerm U, Lichtenecker RJ,
Schanda P. 2026. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic
dopants. Magnetic Resonance. 7(1), 29–37.
mla: Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning
NMR with Paramagnetic Dopants.” Magnetic Resonance, vol. 7, no. 1, Copernicus
Publications, 2026, pp. 29–37, doi:10.5194/mr-7-29-2026.
short: L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker,
P. Schanda, Magnetic Resonance 7 (2026) 29–37.
corr_author: '1'
date_created: 2026-05-03T22:01:36Z
date_published: 2026-04-16T00:00:00Z
date_updated: 2026-05-07T06:49:59Z
day: '16'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.5194/mr-7-29-2026
external_id:
pmid:
- '42057802'
has_accepted_license: '1'
intvolume: ' 7'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.5194/mr-7-29-2026
month: '04'
oa: 1
oa_version: Published Version
page: 29-37
pmid: 1
project:
- _id: B67AFEDC-15C9-11EA-A837-991A96BB2854
name: IST Austria Open Access Fund
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publication: Magnetic Resonance
publication_identifier:
eissn:
- 2699-0016
publication_status: published
publisher: Copernicus Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2026'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '22105'
abstract:
- lang: eng
text: Protein conformational energy landscapes are shaped not only by intramolecular
interactions but also by their environment. In protein crystals and protein–protein
complexes, intermolecular contacts alter this energy landscape, but the exact
nature of this alteration is difficult to decipher. Understanding how the crystal
lattice affects protein dynamics is crucial for crystallography-based studies
of motion, yet its influence on collective motions remains unclear. Aromatic ring
flips in the hydrophobic core represent sensitive probes of such dynamics. Here,
we compare the kinetics of aromatic ring flips in the protein GB1 in crystals,
in complex with its binding partner IgG, and in solution, combining advanced isotope
labelling with quantitative NMR methods. We show that rings in the core flip nearly
a thousand times less frequently in crystals than in solution. Enhanced-sampling
molecular dynamics simulations, based on a crystal structure of a GB1 variant
reported in this work, reproduce these elevated barriers and reveal how the crystal
restrains motions.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: We thank N. R. Skrynnikov and O. O. Lebedenko (St. Petersburg) for
insightful discussions and for performing exploratory MD simulations. We are grateful
to T. Schubeis (Lyon) for advice on GB1 crystallization and R. Schmid for initial
crystallization trials. We thank C. Mueller-Dieckmann for assistance with room-temperature
X-ray crystallography data collection on beamline ID30B at the ESRF, which is acknowledged
for providing beamtime through its In-House Research programme. We thank S. Falkner
for assistance with constructing the structural model of the IgG:GB1 complex. We
thank J. Lewandowski for providing feedback on the paper and granting access to
backbone relaxation data of IgG:GB1T2Q and GB1T2Q microcrystals. This research was
supported by the Scientific Service Units (SSU) of the Institute of Science and
Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance
and the Lab Support Facilities. We thank P. Rovó and M. V. Falcón for excellent
support of the NMR facility. L.M.B. is recipient of a DOC fellowship of the Austrian
Academy of Sciences at the Institute of Science and Technology Austria (grant number
PR10660EAW01). C.C. acknowledges the European Research Council (grant project 101097272
‘MilliInMicro’) and the Métropole du Grand Nancy (grant project ‘ARC’). BM07-FIP2
is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under
grant agreement ANR-21-ESRE-0011.Open access funding provided by Institute of Science
and Technology (IST Austria).
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Haohao
full_name: Fu, Haohao
last_name: Fu
- first_name: Benjamin
full_name: Tatman, Benjamin
id: 71cda2f3-e604-11ee-a1df-da10587eda3f
last_name: Tatman
- first_name: Matthias
full_name: Dreydoppel, Matthias
last_name: Dreydoppel
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Daniel
full_name: Balazs, Daniel
id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E
last_name: Balazs
orcid: 0000-0001-7597-043X
- first_name: Ulrich
full_name: Weininger, Ulrich
last_name: Weininger
- first_name: Sylvain
full_name: Engilberge, Sylvain
last_name: Engilberge
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein
dynamics in crystals and complexes. Nature Chemistry. 2026. doi:10.1038/s41557-026-02155-0
apa: Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs,
D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics
in crystals and complexes. Nature Chemistry. Springer Nature. https://doi.org/10.1038/s41557-026-02155-0
chicago: Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna
Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot,
and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in
Crystals and Complexes.” Nature Chemistry. Springer Nature, 2026. https://doi.org/10.1038/s41557-026-02155-0.
ieee: L. M. Becker et al., “Aromatic ring flips reveal reshaping of protein
dynamics in crystals and complexes,” Nature Chemistry. Springer Nature,
2026.
ista: Becker LM, Fu H, Tatman B, Dreydoppel M, Kapitonova A, Balazs D, Weininger
U, Engilberge S, Chipot C, Schanda P. 2026. Aromatic ring flips reveal reshaping
of protein dynamics in crystals and complexes. Nature Chemistry.
mla: Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein
Dynamics in Crystals and Complexes.” Nature Chemistry, Springer Nature,
2026, doi:10.1038/s41557-026-02155-0.
short: L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U.
Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry (2026).
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: The cryo and room-temperature crystal structures of GB1QDD
are deposited at the PDB under the access codes 9I2I and 9T8Z, respectively. The
solid-state NMR backbone assignment of GB1QDD is deposited at the BMRB under the
access code 53330. NMR spectra, analysis scripts and raw data are publicly available
at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-20641)120. Files
to reproduce the enhanced-sampling MD simulations are publicly available at the
ISTA research explorer (https://doi.org/10.15479/AT-ISTA-21145)121.
date_created: 2026-06-21T22:03:01Z
date_published: 2026-06-10T00:00:00Z
date_updated: 2026-06-24T08:47:58Z
day: '10'
ddc:
- '540'
department:
- _id: PaSc
- _id: LifeSc
doi: 10.1038/s41557-026-02155-0
external_id:
pmid:
- '42271006'
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41557-026-02155-0
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
grant_number: '26777'
name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
approaches
publication: Nature Chemistry
publication_identifier:
eissn:
- '17554349'
issn:
- '17554330'
publication_status: epub_ahead
publisher: Springer Nature
quality_controlled: '1'
related_material:
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relation: research_data
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relation: research_data
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researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2026'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20258'
abstract:
- lang: eng
text: The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise
deuterated proteins holds great potential for high-resolution solution and magic-angle
spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues
play key roles for example at active sites of enzymes. Taking advantage of a chemically
synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we
demonstrate here the usefulness of proton-detected MAS NMR approaches to probe
arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric
enzyme malate dehydrogenase we detected a wide range of motions, from sites that
are rigid on time scales of at least tens of milliseconds to residues undergoing
predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements
enabled quantitative determination of these dynamics. We observed microsecond
dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to
sample different β-turn conformations on this time scale. The labeling scheme
and experiments presented here expand the toolkit for high-resolution proton-detected
MAS NMR.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: This work was supported financially by the Austrian Science Fund
(FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific
Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through
resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support
Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent
support of the NMR facility.
article_number: '169379'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Darja
full_name: Rohden, Darja
id: 81dc668a-19fa-11f0-bf31-d56534059ef3
last_name: Rohden
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Benjamin
full_name: Tatman, Benjamin
id: 71cda2f3-e604-11ee-a1df-da10587eda3f
last_name: Tatman
- first_name: Roman J.
full_name: Lichtenecker, Roman J.
last_name: Lichtenecker
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine
dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme.
Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169379
apa: Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &
Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with
a specific isotope-labeling scheme. Journal of Molecular Biology. Elsevier.
https://doi.org/10.1016/j.jmb.2025.169379
chicago: Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman
J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning
NMR with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology.
Elsevier, 2025. https://doi.org/10.1016/j.jmb.2025.169379.
ieee: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P.
Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific
isotope-labeling scheme,” Journal of Molecular Biology, vol. 437, no. 23.
Elsevier, 2025.
ista: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025.
Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
scheme. Journal of Molecular Biology. 437(23), 169379.
mla: Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR
with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology,
vol. 437, no. 23, 169379, Elsevier, 2025, doi:10.1016/j.jmb.2025.169379.
short: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda,
Journal of Molecular Biology 437 (2025).
corr_author: '1'
date_created: 2025-08-31T22:01:33Z
date_published: 2025-12-01T00:00:00Z
date_updated: 2026-06-10T08:20:37Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1016/j.jmb.2025.169379
external_id:
isi:
- '001618289100020'
file:
- access_level: open_access
checksum: 90d50594d8ea9860ac5da41297992847
content_type: application/pdf
creator: dernst
date_created: 2025-12-29T14:51:40Z
date_updated: 2025-12-29T14:51:40Z
file_id: '20876'
file_name: 2025_JourMolecularBiology_Rohden.pdf
file_size: 2270555
relation: main_file
success: 1
file_date_updated: 2025-12-29T14:51:40Z
has_accepted_license: '1'
intvolume: ' 437'
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issue: '23'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Journal of Molecular Biology
publication_identifier:
eissn:
- 1089-8638
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
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relation: research_data
status: public
scopus_import: '1'
status: public
title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
scheme
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 437
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20538'
abstract:
- lang: eng
text: In this study, we describe an integrated approach for methyl group assignment
comprising precursor-based selective methyl group labeling, a novel pulse sequence
for methyl to backbone coherence transfer and chemical shift predictions using
UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the
adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal
methyl groups of leucine and valine residues to each other and to the protein
backbone. By additional 13C,2H-labeling of residues other than valine and leucine
residues of the protein, important chemical shift information about neighboring
residues (following valine and leucine residues) can be achieved. Thus, different
valine and leucine residues in a protein can be characterized as a specific chemical
shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0
using experimental data taken from a subset of the BMRB database revealed a correct
assignment performance of about 90%. With applications to proteins of 60.2 kDa
and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides
valuable information even for very large proteins.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral
School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B.
This work was supported financially by the Austrian Science Fund (FWF, grant numbers
I06223 and I5812-B, “AlloSpace”). This research was supported by the Scientific
Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through
resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support
Facility (LSF). We thank Celina Sailer for assistance with the analysis of the NMR
spectrum of HsTom70.
article_number: '169465'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Sonja
full_name: Knödlstorfer, Sonja
last_name: Knödlstorfer
- first_name: Giorgia
full_name: Toscano, Giorgia
id: 334a5e40-8747-11f0-b671-ba1f5154b4b4
last_name: Toscano
- first_name: Aleksandra L.
full_name: Ptaszek, Aleksandra L.
last_name: Ptaszek
- first_name: Georg
full_name: Kontaxis, Georg
last_name: Kontaxis
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Jakob
full_name: Schneider, Jakob
id: 64368429-eb97-11eb-a6c2-c980b1f44415
last_name: Schneider
- first_name: Katharina
full_name: Maier, Katharina
last_name: Maier
- first_name: Anna
full_name: Kapitonova, Anna
id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471
last_name: Kapitonova
- first_name: Roman J.
full_name: Lichtenecker, Roman J.
last_name: Lichtenecker
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
citation:
ama: Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy
for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with
UCBShift 2.0. Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169465
apa: Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider,
J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment
using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal
of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2025.169465
chicago: Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis,
Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC
NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate
Integrated with UCBShift 2.0.” Journal of Molecular Biology. Elsevier,
2025. https://doi.org/10.1016/j.jmb.2025.169465.
ieee: S. Knödlstorfer et al., “A novel HMBC-CC-HMQC NMR strategy for methyl
assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift
2.0,” Journal of Molecular Biology, vol. 437, no. 23. Elsevier, 2025.
ista: Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J,
Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC
NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate
integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465.
mla: Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment
Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” Journal
of Molecular Biology, vol. 437, no. 23, 169465, Elsevier, 2025, doi:10.1016/j.jmb.2025.169465.
short: S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider,
K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of
Molecular Biology 437 (2025).
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