---
res:
  bibo_abstract:
  - "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@eng"
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Lea Marie
      foaf_name: Becker, Lea Marie
      foaf_surname: Becker
      foaf_workInfoHomepage: http://www.librecat.org/personId=36336939-eb97-11eb-a6c2-c83f1214ca79
    orcid: 0000-0002-6401-5151
  bibo_doi: 10.15479/AT-ISTA-22334
  dct_date: 2026^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/2663-337X
  - http://id.crossref.org/issn/978-3-99078-084-8
  dct_language: eng
  dct_publisher: Institute of Science and Technology Austria@
  dct_title: Exploring protein dynamics using specific labeling approaches for solid-state
    MAS NMR@
...