---
res:
  bibo_abstract:
  - Aromatic side chains are important reporters of the plasticity of proteins, and
    often form important contacts in protein–protein interactions. We studied aromatic
    residues in the two structurally homologous cross-β amyloid fibrils HET-s, and  HELLF
    by employing a specific isotope-labeling approach and magic-angle-spinning NMR.
    The dynamic behavior of the aromatic residues Phe and Tyr indicates that the hydrophobic
    amyloid core is rigid, without any sign of "breathing motions" over hundreds of
    milliseconds at least. Aromatic residues exposed at the fibril surface have a
    rigid ring axis but undergo ring flips on a variety of time scales from nanoseconds
    to microseconds. Our approach provides direct insight into hydrophobic-core motions,
    enabling a better evaluation of the conformational heterogeneity generated from
    an NMR structural ensemble of such amyloid cross-β architecture.@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
  - foaf_Person:
      foaf_givenName: Paul
      foaf_name: Schanda, Paul
      foaf_surname: Schanda
      foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425
    orcid: 0000-0002-9350-7606
  bibo_doi: 10.15479/AT:ISTA:12497
  dct_date: 2023^xs_gYear
  dct_publisher: Institute of Science and Technology Austria@
  dct_subject:
  - aromatic side chains
  - isotopic labeling
  - protein dynamics
  - ring flips
  - spin relaxation
  dct_title: 'Research data to: The rigid core and flexible surface of amyloid fibrils
    probed by magic-angle-spinning NMR spectroscopy of aromatic residues@'
...