---
OA_place: publisher
OA_type: hybrid
_id: '22974'
abstract:
- lang: eng
  text: Far from being static structures, it is now well accepted that proteins are
    highly dynamic entities even in the solid state. Here, we review recent progress
    in application of magic-angle spinning (MAS) NMR for studying the site-specific
    dynamics of proteins, as assessed using spin-relaxation and measurement of anisotropic
    spin interactions. We focus on the types of experimental data that are available,
    and how best to access the information which is provided by these experimental
    measurements; in particular, we provide a retrospective on the field in light
    of recent advances in analytical methodologies, which have led to a slow paradigm
    shift in how we interpret relaxation rate constant measurements made in the solid
    state.
acknowledgement: We thank the Austrian Science Fund (FWF, project number 10.55776/I5812)
  for support. We are grateful to Petra Rovó (ISTA) for many insightful discussions.
article_number: '101615'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Benjamin
  full_name: Tatman, Benjamin
  id: 71cda2f3-e604-11ee-a1df-da10587eda3f
  last_name: Tatman
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Tatman B, Schanda P. Quantifying fast protein dynamics by magic-angle spinning
    NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear
    Magnetic Resonance Spectroscopy</i>. 2026;156-157. doi:<a href="https://doi.org/10.1016/j.pnmrs.2026.101615">10.1016/j.pnmrs.2026.101615</a>'
  apa: 'Tatman, B., &#38; Schanda, P. (2026). Quantifying fast protein dynamics by
    magic-angle spinning NMR: Progress in experimental and analytical approaches.
    <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier. <a href="https://doi.org/10.1016/j.pnmrs.2026.101615">https://doi.org/10.1016/j.pnmrs.2026.101615</a>'
  chicago: 'Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics
    by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.”
    <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier, 2026. <a
    href="https://doi.org/10.1016/j.pnmrs.2026.101615">https://doi.org/10.1016/j.pnmrs.2026.101615</a>.'
  ieee: 'B. Tatman and P. Schanda, “Quantifying fast protein dynamics by magic-angle
    spinning NMR: Progress in experimental and analytical approaches,” <i>Progress
    in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157. Elsevier, 2026.'
  ista: 'Tatman B, Schanda P. 2026. Quantifying fast protein dynamics by magic-angle
    spinning NMR: Progress in experimental and analytical approaches. Progress in
    Nuclear Magnetic Resonance Spectroscopy. 156–157, 101615.'
  mla: 'Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by
    Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.”
    <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157, 101615,
    Elsevier, 2026, doi:<a href="https://doi.org/10.1016/j.pnmrs.2026.101615">10.1016/j.pnmrs.2026.101615</a>.'
  short: B. Tatman, P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy
    156–157 (2026).
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: No data was used for the research described in the article.
date_created: 2026-09-22T05:44:22Z
date_published: 2026-09-01T00:00:00Z
date_updated: 2026-10-06T13:00:47Z
day: '01'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1016/j.pnmrs.2026.101615
fulldoi: https://doi.org/10.1016/j.pnmrs.2026.101615
has_accepted_license: '1'
keyword:
- Solid-state NMR
- Protein dynamics
- Magic-angle spinning
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.pnmrs.2026.101615
month: '09'
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: Progress in Nuclear Magnetic Resonance Spectroscopy
publication_identifier:
  eissn:
  - 1873-3301
  issn:
  - 0079-6565
publication_status: epub_ahead
publisher: Elsevier
quality_controlled: '1'
researchdata_availability: no
scopus_import: '1'
status: public
supplementarymaterial: yes
title: 'Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in
  experimental and analytical approaches'
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: 156-157
year: '2026'
...