---
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.
    <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href="https://doi.org/10.1016/j.jmb.2025.169379">10.1016/j.jmb.2025.169379</a>
  apa: Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38;
    Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with
    a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.jmb.2025.169379">https://doi.org/10.1016/j.jmb.2025.169379</a>
  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.” <i>Journal of Molecular Biology</i>.
    Elsevier, 2025. <a href="https://doi.org/10.1016/j.jmb.2025.169379">https://doi.org/10.1016/j.jmb.2025.169379</a>.
  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,” <i>Journal of Molecular Biology</i>, 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.” <i>Journal of Molecular Biology</i>,
    vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href="https://doi.org/10.1016/j.jmb.2025.169379">10.1016/j.jmb.2025.169379</a>.
  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'
isi: 1
issue: '23'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
  grant_number: I05812
  name: AlloSpace. The emergence and mechanisms of allostery
publication: Journal of Molecular Biology
publication_identifier:
  eissn:
  - 1089-8638
  issn:
  - 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
  record:
  - id: '19956'
    relation: research_data
    status: public
scopus_import: '1'
status: public
title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling
  scheme
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 437
year: '2025'
...
---
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. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href="https://doi.org/10.1016/j.jmb.2025.169465">10.1016/j.jmb.2025.169465</a>
  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. <i>Journal
    of Molecular Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmb.2025.169465">https://doi.org/10.1016/j.jmb.2025.169465</a>
  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.” <i>Journal of Molecular Biology</i>. Elsevier,
    2025. <a href="https://doi.org/10.1016/j.jmb.2025.169465">https://doi.org/10.1016/j.jmb.2025.169465</a>.
  ieee: S. Knödlstorfer <i>et al.</i>, “A novel HMBC-CC-HMQC NMR strategy for methyl
    assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift
    2.0,” <i>Journal of Molecular Biology</i>, 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.” <i>Journal
    of Molecular Biology</i>, vol. 437, no. 23, 169465, Elsevier, 2025, doi:<a href="https://doi.org/10.1016/j.jmb.2025.169465">10.1016/j.jmb.2025.169465</a>.
  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
  content_type: application/pdf
  creator: dernst
  date_created: 2025-12-30T10:29:08Z
  date_updated: 2025-12-30T10:29:08Z
  file_id: '20915'
  file_name: 2025_JourMolecularBiology_Knoedlstorfer.pdf
  file_size: 3076611
  relation: main_file
  success: 1
file_date_updated: 2025-12-30T10:29:08Z
has_accepted_license: '1'
intvolume: '       437'
issue: '23'
language:
- iso: eng
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'
...
---
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. <i>Magnetic Resonance</i>. 2024;5(1):33-49. doi:<a
    href="https://doi.org/10.5194/mr-5-33-2024">10.5194/mr-5-33-2024</a>'
  apa: 'Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C.,
    &#38; Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution
    amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck.
    <i>Magnetic Resonance</i>. Copernicus Publications. <a href="https://doi.org/10.5194/mr-5-33-2024">https://doi.org/10.5194/mr-5-33-2024</a>'
  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.” <i>Magnetic Resonance</i>. Copernicus Publications,
    2024. <a href="https://doi.org/10.5194/mr-5-33-2024">https://doi.org/10.5194/mr-5-33-2024</a>.'
  ieee: 'F. Napoli <i>et al.</i>, “Deuteration of proteins boosted by cell lysates:
    High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation
    bottleneck,” <i>Magnetic Resonance</i>, 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.” <i>Magnetic Resonance</i>, vol. 5, no. 1, Copernicus Publications,
    2024, pp. 33–49, doi:<a href="https://doi.org/10.5194/mr-5-33-2024">10.5194/mr-5-33-2024</a>.'
  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: 2025-07-17T08:12:23Z
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
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'
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'
...
---
_id: '14036'
abstract:
- lang: eng
  text: Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing
    itself as a powerful method for the characterization of protein dynamics at the
    atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore
    microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling,
    and pulse sequence design has paved the way for quantitative analyses of even
    rare structural fluctuations. In addition to isotropic chemical-shift fluctuations
    exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has
    a wider arsenal of observables, allowing to see motions even if the exchanging
    states do not differ in their chemical shifts. We demonstrate the potential of
    the technique for probing motions in challenging large enzymes, membrane proteins,
    and protein assemblies.
acknowledgement: We thank Petra Rovó for critical reading of this manuscript. We acknowledge
  the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding
  by the Institute of Science and Technology Austria.
article_number: '102660'
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author:
- first_name: Federico
  full_name: Napoli, Federico
  id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
  last_name: Napoli
  orcid: 0000-0002-9043-136X
- first_name: Lea Marie
  full_name: Becker, Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning
    relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10).
    doi:<a href="https://doi.org/10.1016/j.sbi.2023.102660">10.1016/j.sbi.2023.102660</a>
  apa: Napoli, F., Becker, L. M., &#38; Schanda, P. (2023). Protein dynamics detected
    by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2023.102660">https://doi.org/10.1016/j.sbi.2023.102660</a>
  chicago: Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics
    Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion
    in Structural Biology</i>. Elsevier, 2023. <a href="https://doi.org/10.1016/j.sbi.2023.102660">https://doi.org/10.1016/j.sbi.2023.102660</a>.
  ieee: F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle
    spinning relaxation dispersion NMR,” <i>Current Opinion in Structural Biology</i>,
    vol. 82, no. 10. Elsevier, 2023.
  ista: Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle
    spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10),
    102660.
  mla: Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning
    Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>, vol.
    82, no. 10, 102660, Elsevier, 2023, doi:<a href="https://doi.org/10.1016/j.sbi.2023.102660">10.1016/j.sbi.2023.102660</a>.
  short: F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology
    82 (2023).
corr_author: '1'
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2025-04-14T09:10:17Z
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ddc:
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department:
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doi: 10.1016/j.sbi.2023.102660
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title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
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