Dynamical crossover of water confined within the amphiphilic nanocores of aggregated amyloid β peptides
Author:
Affiliation:
1. Molecular Modeling Laboratory, Department of Chemistry
2. Indian Institute of Technology
3. Kharagpur-721302
4. India
5. Centre for Computational and Data Sciences
Abstract
The size-dependent structural crossover of Aβ protofilaments at the decamer is associated with correlated dynamical transition of water confined within its amphiphilic core.
Funder
University Grants Commission
Department of Science and Technology, Ministry of Science and Technology
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP01942H
Reference67 articles.
1. D. L. Nelson , A. L.Lehninger and M. M.Cox , Lehninger Principles of Biochemistry , Macmillan , 2008
2. Molecular chaperones in protein folding and proteostasis
3. Intrinsically Disordered Proteins in Human Diseases: Introducing the D2 Concept
4. Protein Misfolding, Functional Amyloid, and Human Disease
5. Regulation of APP cleavage by α-, β- and γ-secretases
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