---
_id: '12497'
abstract:
- lang: eng
  text: 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.
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
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Becker LM, Schanda P. Research data to: The rigid core and flexible surface
    of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic
    residues. 2023. doi:<a href="https://doi.org/10.15479/AT:ISTA:12497">10.15479/AT:ISTA:12497</a>'
  apa: 'Becker, L. M., &#38; Schanda, P. (2023). Research data to: The rigid core
    and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy
    of aromatic residues. Institute of Science and Technology Austria. <a href="https://doi.org/10.15479/AT:ISTA:12497">https://doi.org/10.15479/AT:ISTA:12497</a>'
  chicago: 'Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core
    and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
    of Aromatic Residues.” Institute of Science and Technology Austria, 2023. <a href="https://doi.org/10.15479/AT:ISTA:12497">https://doi.org/10.15479/AT:ISTA:12497</a>.'
  ieee: 'L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible
    surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
    aromatic residues.” Institute of Science and Technology Austria, 2023.'
  ista: 'Becker LM, Schanda P. 2023. Research data to: The rigid core and flexible
    surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
    aromatic residues, Institute of Science and Technology Austria, <a href="https://doi.org/10.15479/AT:ISTA:12497">10.15479/AT:ISTA:12497</a>.'
  mla: 'Becker, Lea Marie, and Paul Schanda. <i>Research Data to: The Rigid Core and
    Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
    of Aromatic Residues</i>. Institute of Science and Technology Austria, 2023, doi:<a
    href="https://doi.org/10.15479/AT:ISTA:12497">10.15479/AT:ISTA:12497</a>.'
  short: L.M. Becker, P. Schanda, (2023).
contributor:
- contributor_type: researcher
  first_name: Mélanie
  last_name: Berbon
- contributor_type: researcher
  first_name: Alicia
  last_name: Vallet
- contributor_type: researcher
  first_name: Axelle
  last_name: Grelard
- contributor_type: researcher
  first_name: Estelle
  last_name: Morvan
- contributor_type: researcher
  first_name: Benjamin
  last_name: Bardiaux
- contributor_type: researcher
  first_name: Roman
  last_name: Lichtenecker
- contributor_type: researcher
  first_name: Matthias
  last_name: Ernst
- contributor_type: researcher
  first_name: Antoine
  last_name: Loquet
- contributor_type: contact_person
  first_name: Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- contributor_type: researcher
  first_name: Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
date_created: 2023-02-03T08:08:02Z
date_published: 2023-03-23T00:00:00Z
date_updated: 2024-02-21T12:14:06Z
day: '23'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT:ISTA:12497
file:
- access_level: open_access
  checksum: fd9a28620a81a82991fb70f4fd6591d9
  content_type: application/zip
  creator: lbecker
  date_created: 2023-03-23T10:03:16Z
  date_updated: 2023-03-24T09:34:20Z
  file_id: '12743'
  file_name: Research_Data.zip
  file_size: 87018103
  relation: main_file
- access_level: open_access
  checksum: 30ebdfb600af118fcf8518b6efe0b7e9
  content_type: text/plain
  creator: dernst
  date_created: 2023-03-24T07:13:55Z
  date_updated: 2023-03-24T09:42:03Z
  file_id: '12755'
  file_name: README.txt
  file_size: 747
  relation: main_file
file_date_updated: 2023-03-24T09:42:03Z
has_accepted_license: '1'
keyword:
- aromatic side chains
- isotopic labeling
- protein dynamics
- ring flips
- spin relaxation
month: '03'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
  record:
  - id: '12675'
    relation: used_in_publication
    status: public
status: public
title: 'Research data to: The rigid core and flexible surface of amyloid fibrils probed
  by magic-angle-spinning NMR spectroscopy of aromatic residues'
tmp:
  image: /images/cc_by_nc.png
  legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
  short: CC BY-NC (4.0)
type: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...