Paramagnetic relaxation enhancement-assisted structural characterization of a partially disordered conformation of ubiquitin.


Journal

Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750

Informations de publication

Date de publication:
11 2019
Historique:
received: 28 06 2019
revised: 18 09 2019
accepted: 19 09 2019
pubmed: 7 10 2019
medline: 16 7 2020
entrez: 7 10 2019
Statut: ppublish

Résumé

Nuclear magnetic resonance (NMR) is a powerful tool to study three-dimensional structures as well as protein conformational fluctuations in solution, but it is compromised by increases in peak widths and missing signals. We previously reported that ubiquitin has two folded conformations, N

Identifiants

pubmed: 31587403
doi: 10.1002/pro.3734
pmc: PMC6798129
doi:

Substances chimiques

Ubiquitin 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1993-2003

Informations de copyright

© 2019 The Protein Society.

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Auteurs

Takuro Wakamoto (T)

Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.

Teppei Ikeya (T)

Tokyo Metropolitan University, Hachioji, Tokyo, Japan.

Soichiro Kitazawa (S)

College of Pharmaceutical Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.

Nicola J Baxter (NJ)

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.

Mike P Williamson (MP)

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.

Ryo Kitahara (R)

Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.
College of Pharmaceutical Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.

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Classifications MeSH