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Title: Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy.
Authors: Yamaguchi, Takahiro
Matsuzaki, Katsumi  kyouindb  KAKEN_id  orcid (unconfirmed)
Hoshino, Masaru  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 星野, 大
Keywords: NMR
Amyloid fibril formation
Conformational change
Chemical exchange
Issue Date: 6-Apr-2011
Publisher: Elsevier B.V.
Journal title: FEBS letters
Volume: 585
Issue: 7
Start page: 1097
End page: 1102
Abstract: A detailed analysis of the NMR spectra of amyloid-β (Aβ) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of Aβ aggregation, each molecule might adopt transiently a turn conformation at around D23-A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a "nucleus" for amyloid fibrils.
Rights: © 2011 Federation of European Biochemical Societies Published by Elsevier B.V.
This is not the published version. Please cite only the published version.
DOI(Published Version): 10.1016/j.febslet.2011.03.014
PubMed ID: 21402073
Appears in Collections:Journal Articles

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