---
OA_place: publisher
_id: '22334'
abstract:
- lang: eng
  text: "Characterizing protein dynamics at the atomic level is essential for our
    understanding of biological mechanisms. Whether it is to facilitate metabolite
    transport, catalyze reactions, transmit signals, or regulate metabolism – proteins
    are constantly in motion and sample multiple conformational states to fulfill
    their function. Nuclear magnetic resonance (NMR) spectroscopy is particularly
    well suited to elucidate the dynamics of biomolecules on their complex free-energy
    landscape. In particular, solid-state magic-angle spinning (MAS) NMR enables the
    study of large molecular assemblies, protein crystals, or insoluble proteins at
    atomic resolution without an inherent molecular size limitation. MAS NMR experiments
    to probe protein dynamics are extremely versatile and sensitive to motional timescales
    from picoseconds to seconds. Over the past decades, technological advances, developments
    in experimental design, and new isotope-labeling approaches have further expanded
    the possibilities of this technique and significantly improved the accuracy of
    the determined motional parameters.\r\nFunctionally important sites of proteins
    often contain aromatic residues. Their side-chain motions have therefore long
    served as valuable indicators of mechanistically relevant dynamics in NMR studies.
    In this thesis, site-specifically labeled aromatic residues act as sensitive reporters
    for MAS NMR studies of protein dynamics. The first part addresses how different
    environments impact side-chain motion by probing ring flips of phenylalanines
    and tyrosines in crystalline proteins and amyloid fibrils. It provides important
    insights for the analysis of dynamics obtained in non-native protein environments
    and emphasizes the complex factors that determine the timescale of internal dynamics.
    In the second part, the focus shifts towards methodological questions regarding
    the investigation of protein dynamics by 19F MAS NMR. The fluorine nucleus exhibits
    promising characteristics for NMR studies but also presents significant challenges,
    which is why the full methodological potential of 19F MAS NMR has not been fully
    realized yet. This work demonstrates that paramagnetic doping can considerably
    reduce the measurement time and improve the sensitivity of fluorinated samples.
    Finally, 19F MAS NMR is evaluated as a tool for studying protein side-chain dynamics
    on the example of tryptophans. The results illustrate the challenges in analyzing
    such experiments and lay the foundation for further development of 19F MAS NMR
    relaxation studies.\r\nTaken together, this thesis highlights the potential of
    combining specific isotope labeling, MAS NMR, and complementary methods such as
    crystallography and computational simulations to elucidate internal protein dynamics.
    The further development of such integrative approaches will be crucial to improving
    our understanding of complex mechanisms and protein function.\r\n"
acknowledged_ssus:
- _id: LifeSc
- _id: NMR
acknowledgement: "During the work on this thesis, I was the recipient of a DOC Fellowship
  of the Austrian\r\nAcademy of Sciences at the Institute of Science and Technology
  Austria (grant no. PR10660EAW01)."
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Lea Marie
  full_name: Becker, Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
citation:
  ama: Becker LM. Exploring protein dynamics using specific labeling approaches for
    solid-state MAS NMR. 2026. doi:<a href="https://doi.org/10.15479/AT-ISTA-22334">10.15479/AT-ISTA-22334</a>
  apa: Becker, L. M. (2026). <i>Exploring protein dynamics using specific labeling
    approaches for solid-state MAS NMR</i>. Institute of Science and Technology Austria.
    <a href="https://doi.org/10.15479/AT-ISTA-22334">https://doi.org/10.15479/AT-ISTA-22334</a>
  chicago: Becker, Lea Marie. “Exploring Protein Dynamics Using Specific Labeling
    Approaches for Solid-State MAS NMR.” Institute of Science and Technology Austria,
    2026. <a href="https://doi.org/10.15479/AT-ISTA-22334">https://doi.org/10.15479/AT-ISTA-22334</a>.
  ieee: L. M. Becker, “Exploring protein dynamics using specific labeling approaches
    for solid-state MAS NMR,” Institute of Science and Technology Austria, 2026.
  ista: Becker LM. 2026. Exploring protein dynamics using specific labeling approaches
    for solid-state MAS NMR. Institute of Science and Technology Austria.
  mla: Becker, Lea Marie. <i>Exploring Protein Dynamics Using Specific Labeling Approaches
    for Solid-State MAS NMR</i>. Institute of Science and Technology Austria, 2026,
    doi:<a href="https://doi.org/10.15479/AT-ISTA-22334">10.15479/AT-ISTA-22334</a>.
  short: L.M. Becker, Exploring Protein Dynamics Using Specific Labeling Approaches
    for Solid-State MAS NMR, Institute of Science and Technology Austria, 2026.
corr_author: '1'
das_tickbox: '1'
date_created: 2026-07-14T08:08:51Z
date_published: 2026-07-13T00:00:00Z
date_updated: 2026-07-20T09:49:13Z
day: '13'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT-ISTA-22334
doi_confirm: '1'
file:
- access_level: closed
  checksum: 8b85114eff543916c0e1445cd2189555
  content_type: application/zip
  creator: lbecker
  date_created: 2026-07-16T09:17:08Z
  date_updated: 2026-07-16T09:17:08Z
  file_id: '22346'
  file_name: 2026_Becker_Lea_source_files.zip
  file_size: 99472908
  relation: source_file
- access_level: open_access
  checksum: 6c526862bc6dbd1e4c80ecb34580bc58
  content_type: application/pdf
  creator: lbecker
  date_created: 2026-07-16T09:17:05Z
  date_updated: 2026-07-16T09:17:05Z
  file_id: '22347'
  file_name: 2026_Becker_Lea_Thesis.pdf
  file_size: 74647289
  relation: main_file
  success: 1
file_date_updated: 2026-07-16T09:17:08Z
has_accepted_license: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '07'
oa: 1
oa_version: Published Version
page: '205'
project:
- _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0
  grant_number: '26777'
  name: Exploring protein dynamics by solid-state MAS NMR through specific labeling
    approaches
publication_identifier:
  isbn:
  - 978-3-99078-084-8
  issn:
  - 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
  record:
  - id: '22105'
    relation: part_of_dissertation
    status: public
  - id: '12675'
    relation: part_of_dissertation
    status: public
  - id: '21777'
    relation: part_of_dissertation
    status: public
  - id: '12114'
    relation: part_of_dissertation
    status: public
status: public
supervisor:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
title: Exploring protein dynamics using specific labeling approaches for solid-state
  MAS NMR
tmp:
  image: /images/cc_by_nc_nd.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
    (CC BY-NC-ND 4.0)
  short: CC BY-NC-ND (4.0)
type: dissertation
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2026'
...