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

Structure

Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany; Bavarian NMR Center and Center for Integrated Protein Science Munich at Department Chemie, Technical University of Munich, Garching, Germany. Electronic address:

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

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http://dx.doi.org/10.1016/j.str.2020.06.005DOI Listing

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