---
_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'
article_processing_charge: Yes (via OA deal)
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: 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).
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2024-01-30T12:37:36Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.sbi.2023.102660
external_id:
  isi:
  - '001053616200001'
  pmid:
  - '37536064'
file:
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  date_created: 2024-01-30T12:36:39Z
  date_updated: 2024-01-30T12:36:39Z
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intvolume: '        82'
isi: 1
issue: '10'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
  grant_number: I05812
  name: AlloSpace. The emergence and mechanisms of allostery
publication: Current Opinion in Structural Biology
publication_identifier:
  eissn:
  - 1879-033X
  issn:
  - 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 82
year: '2023'
...