Induced Dipole–Dipole Interactions Influence the Unfolding Pathways of Wild-Type and Mutant Amyloid β-Peptides
Author:
Affiliation:
1. Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5b09978
Reference59 articles.
1. Unfolding the role of protein misfolding in neurodegenerative diseases
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4. Charge Alterations of E22 Enhance the Pathogenic Properties of the Amyloid β-Protein
5. Substitutions at codon 22 of Alzheimer's A beta peptide induce conformational changes and diverse apoptotic effects in human cerebral endothelial cells
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