---
_id: '8447'
abstract:
- lang: eng
  text: 'Solid-state NMR spectroscopy can provide site-resolved information about
    protein dynamics over many time scales. Here we combine protein deuteration, fast
    magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin
    in microcrystals, and in particular a mutant in a region that undergoes microsecond
    motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation
    measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation
    dispersion, to probe how the G53A mutation alters these dynamics. We report a
    population-inversion of conformational states: the conformation that in the wild-type
    protein is populated only sparsely becomes the predominant state. We furthermore
    explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics.
    We show that while quantitative interpretation of 1H relaxation remains beyond
    reach under the experimental conditions, due to coherent contributions to decay,
    one may extract qualitative information about flexibility.'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Petra
  full_name: Rovó, Petra
  last_name: Rovó
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Rasmus
  full_name: Linser, Rasmus
  last_name: Linser
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational
    dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type
    and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95.
    doi:<a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">10.1016/j.ssnmr.2017.04.002</a>'
  apa: 'Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda,
    P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation
    dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State
    Nuclear Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>'
  chicago: 'Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser,
    and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation
    Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State
    Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>.'
  ieee: 'D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda,
    “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
    Application to wild-type and G53A ubiquitin crystals,” <i>Solid State Nuclear
    Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.'
  ista: 'Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein
    conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application
    to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance.
    87(10), 86–95.'
  mla: 'Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and
    1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.”
    <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017,
    pp. 86–95, doi:<a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">10.1016/j.ssnmr.2017.04.002</a>.'
  short: D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid
    State Nuclear Magnetic Resonance 87 (2017) 86–95.
date_created: 2020-09-18T10:06:18Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.ssnmr.2017.04.002
extern: '1'
intvolume: '        87'
issue: '10'
keyword:
- Nuclear and High Energy Physics
- Instrumentation
- General Chemistry
- Radiation
language:
- iso: eng
month: '10'
oa_version: None
page: 86-95
publication: Solid State Nuclear Magnetic Resonance
publication_identifier:
  issn:
  - 0926-2040
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
  Application to wild-type and G53A ubiquitin crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 87
year: '2017'
...