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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

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The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain

Sandra Hoefgen1, Sven O Dahms1, Kathrin Oertwig1

  • 1Protein Crystallography Group, Leibniz Institute for Age Research, Fritz Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.

Journal of Molecular Biology
|December 22, 2014
PubMed
Summary

Alzheimer's disease (AD) research shows that the amyloid precursor protein (APP) changes shape based on pH. This pH-dependent conformational switch in APP-E1 may offer new therapeutic strategies for AD.

Keywords:
Alzheimer's diseasecrystal structuredynamic light scatteringmerohedral twinningpH dependence

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