---
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: 2026-07-20T09:49:12Z
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'
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scopus_import: '1'
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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: '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: 2025-12-30T10:29:20Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.1016/j.jmb.2025.169465
external_id:
pmid:
- '41016549'
file:
- access_level: open_access
checksum: feb92f9c79032c261165f4ca573f444a
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creator: dernst
date_created: 2025-12-30T10:29:08Z
date_updated: 2025-12-30T10:29:08Z
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file_size: 3076611
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has_accepted_license: '1'
intvolume: ' 437'
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language:
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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'
...