When Less Is More: Combining Site-Specific Isotope Labeling and NMR Unravels Structural Details of Huntingtin Repeats

Florent Delhommel; Michael Sattler

doi:10.1016/j.str.2020.06.005

When Less Is More: Combining Site-Specific Isotope Labeling and NMR Unravels Structural Details of Huntingtin Repeats

Florent Delhommel, Michael Sattler

Chair of Biomolecular NMR-Spectroscopy

Research output: Contribution to journal › Comment/debate

Abstract

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 α-helical conformation while a following proline-rich region favors extended conformations.

Original language	English
Pages (from-to)	730-732
Number of pages	3
Journal	Structure
Volume	28
Issue number	7
DOIs	https://doi.org/10.1016/j.str.2020.06.005
State	Published - 7 Jul 2020

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10.1016/j.str.2020.06.005

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title = "When Less Is More: Combining Site-Specific Isotope Labeling and NMR Unravels Structural Details of Huntingtin Repeats",

abstract = "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 α-helical conformation while a following proline-rich region favors extended conformations.",

author = "Florent Delhommel and Michael Sattler",

note = "Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",

year = "2020",

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language = "English",

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T2 - Combining Site-Specific Isotope Labeling and NMR Unravels Structural Details of Huntingtin Repeats

AU - Delhommel, Florent

AU - Sattler, Michael

PY - 2020/7/7

Y1 - 2020/7/7

N2 - 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 α-helical conformation while a following proline-rich region favors extended conformations.

AB - 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 α-helical conformation while a following proline-rich region favors extended conformations.

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DO - 10.1016/j.str.2020.06.005

M3 - Comment/debate

C2 - 32640252

AN - SCOPUS:85087037606

SN - 0969-2126

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EP - 732

JO - Structure

JF - Structure

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ER -

When Less Is More: Combining Site-Specific Isotope Labeling and NMR Unravels Structural Details of Huntingtin Repeats

Abstract

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