Hydrogen Bonding in Alzheimer’s Amyloid-β Fibrils Probed by15N{17O} REAPDOR Solid-State NMR Spectroscopy

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Abstract

An exclusive label: 15N{17O} REAPDOR NMR was used to validate intermolecular C17O⋅⋅⋅H15N hydrogen bonding in Ac-Aβ(16–22)-NH2 (see scheme) and Aβ(11–25) amyloid fibrils, which are associated with Alzheimer's disease, by selectively labeling them with 17O and 15N. This method was effective for confirming the structure of these fibrils, and could be useful for a number of other biological samples.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Physics
Library of Congress Subject Headings (LCSH): Hydrogen bonding, Amyloid, Alzheimer's disease -- Physiological aspects
Journal or Publication Title: Angewandte Chemie International Edition
Publisher: Wiley - V C H Verlag GmbH & Co. KGaA
ISSN: 1433-7851
Official Date: 2012
Dates:
Date
Event
2012
Published
Volume: Vol. 51
Number: No. 41
Page Range: pp. 10289-10292
DOI: 10.1002/anie.201203595
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
RIOXX Funder/Project Grant:
Project/Grant ID
RIOXX Funder Name
Funder ID
UNSPECIFIED
[EPSRC] Engineering and Physical Sciences Research Council
Related URLs:
URI: https://wrap.warwick.ac.uk/52025/

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