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When less is more: Combining site-specific isotope labeling and NMR unravels structural details of huntingtin repeats.
Structure 28, 730-732 (2020)
In this issue of Structure, Urbanek et al. (2020a) combine site-specific isotope labeling and NMR spectroscopy to investigate opposing effects of flanking regions onto the conformation of the poly-Q region in Huntingtin. Poly-Q interactions with preceding residues promote an a-helical conformation while a following proline-rich region favors extended conformations.
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Publication type
Article: Journal article
Document type
Editorial
Language
english
Publication Year
2020
HGF-reported in Year
2020
ISSN (print) / ISBN
0969-2126
e-ISSN
1878-4186
Journal
Structure
Quellenangaben
Volume: 28,
Issue: 7,
Pages: 730-732
Publisher
Cell Press
Publishing Place
50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-001
WOS ID
WOS:000548064000002
Scopus ID
85087037606
Erfassungsdatum
2020-07-23