Distinct Conformational States of the Alzheimer β‐Amyloid Peptide Can Be Detected by High‐Pressure NMR Spectroscopy1. Issue 34 (10th July 2013)

• Record Type: Journal Article
• Authors: Munte, Claudia Elisabeth; Beck Erlach, Markus; Kremer, Werner; Koehler, Joerg; Kalbitzer, Hans Robert
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 34(2013)
• Page Start: 8943
• Page End: 8947
• Publication Date: 2013-07-10
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201301537
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Folding under pressure</bold>: High‐pressure NMR spectroscopy detects three different conformational states of the Aβ‐peptide in solution: a compactly folded state <bold>1</bold>, a partially folded state <bold>2′</bold>, and a random‐coil like state <bold>2′′</bold> (see plot, p=population). At ambient pressure the folded state <bold>1</bold> dominates which probably has a high affinity to fibrils and thus may promote fibril formation.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg36jz84nw" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>