Linked Life Data

21402073

Source:http://linkedlifedata.com/resource/pubmed/id/21402073

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-4-4
pubmed:abstractText
A detailed analysis of the NMR spectra of amyloid-? (A?) 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 A? 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1873-3468
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
585
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1097-102
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Transient formation of intermediate conformational states of amyloid-? peptide revealed by heteronuclear magnetic resonance spectroscopy.
pubmed:affiliation
Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't