---
_id: '8455'
abstract:
- lang: eng
  text: Solid-state NMR spectroscopy allows the characterization of the structure,
    interactions and dynamics of insoluble and/or very large proteins. Sensitivity
    and resolution are often major challenges for obtaining atomic-resolution information,
    in particular for very large protein complexes. Here we show that the use of deuterated,
    specifically CH3-labelled proteins result in significant sensitivity gains compared
    to previously employed CHD2 labelling, while line widths increase only marginally.
    We apply this labelling strategy to a 468 kDa-large dodecameric aminopeptidase,
    TET2, and the 1.6 MDa-large 50S ribosome subunit of Thermus thermophilus.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Elodie
  full_name: Crublet, Elodie
  last_name: Crublet
- first_name: Pavel
  full_name: Macek, Pavel
  last_name: Macek
- first_name: Rime
  full_name: Kerfah, Rime
  last_name: Kerfah
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Jérôme
  full_name: Boisbouvier, Jérôme
  last_name: Boisbouvier
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state
    NMR spectroscopy of large proteins with selective CH3labelling: Application to
    the 50S ribosome subunit. <i>Chemical Communications</i>. 2016;52(61):9558-9561.
    doi:<a href="https://doi.org/10.1039/c6cc04484k">10.1039/c6cc04484k</a>'
  apa: 'Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier,
    J., &#38; Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy
    of large proteins with selective CH3labelling: Application to the 50S ribosome
    subunit. <i>Chemical Communications</i>. Royal Society of Chemistry. <a href="https://doi.org/10.1039/c6cc04484k">https://doi.org/10.1039/c6cc04484k</a>'
  chicago: 'Kurauskas, Vilius, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F.
    Gauto, Jérôme Boisbouvier, and Paul Schanda. “Sensitive Proton-Detected Solid-State
    NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to
    the 50S Ribosome Subunit.” <i>Chemical Communications</i>. Royal Society of Chemistry,
    2016. <a href="https://doi.org/10.1039/c6cc04484k">https://doi.org/10.1039/c6cc04484k</a>.'
  ieee: 'V. Kurauskas <i>et al.</i>, “Sensitive proton-detected solid-state NMR spectroscopy
    of large proteins with selective CH3labelling: Application to the 50S ribosome
    subunit,” <i>Chemical Communications</i>, vol. 52, no. 61. Royal Society of Chemistry,
    pp. 9558–9561, 2016.'
  ista: 'Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda
    P. 2016. Sensitive proton-detected solid-state NMR spectroscopy of large proteins
    with selective CH3labelling: Application to the 50S ribosome subunit. Chemical
    Communications. 52(61), 9558–9561.'
  mla: 'Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy
    of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome
    Subunit.” <i>Chemical Communications</i>, vol. 52, no. 61, Royal Society of Chemistry,
    2016, pp. 9558–61, doi:<a href="https://doi.org/10.1039/c6cc04484k">10.1039/c6cc04484k</a>.'
  short: V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier,
    P. Schanda, Chemical Communications 52 (2016) 9558–9561.
date_created: 2020-09-18T10:07:29Z
date_published: 2016-07-04T00:00:00Z
date_updated: 2021-01-12T08:19:23Z
day: '04'
doi: 10.1039/c6cc04484k
extern: '1'
intvolume: '        52'
issue: '61'
keyword:
- Materials Chemistry
- Electronic
- Optical and Magnetic Materials
- General Chemistry
- Surfaces
- Coatings and Films
- Metals and Alloys
- Ceramics and Composites
- Catalysis
language:
- iso: eng
month: '07'
oa_version: None
page: 9558-9561
publication: Chemical Communications
publication_identifier:
  issn:
  - 1359-7345
  - 1364-548X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: 'Sensitive proton-detected solid-state NMR spectroscopy of large proteins with
  selective CH3labelling: Application to the 50S ribosome subunit'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 52
year: '2016'
...