View : 17 Download: 0

Full metadata record

DC FieldValueLanguage
dc.contributor.author이민영-
dc.date.accessioned2018-05-02T08:15:49Z-
dc.date.available2018-05-02T08:15:49Z-
dc.date.issued2004-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/242817-
dc.description.abstractWe have observed the conformation switching of Aβ11-25 in the course of amyloid aggregation by employing time-resolved fluorescence resonance energy transfer (FRET). The amyloid peptides undergo multi-step conformational changes during self-assembling such as random coil (monomers), collapsed coil (multimers), micellar structure, and extended β-sheet in fibrils. We first identified the critical micelle concentration of Aβ 11-25 that occurs at ca. 3μM for pH 5.0 and ca. 70μM for pH 7.4. Our experimental results show clearly that the end-to-end distance of micellar Aβ11-25 becomes much shorter than that of the collapsed coil or fibril structure. © 2004 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.titleObservation of multi-step conformation switching in β-amyloid peptide aggregation by fluorescence resonance energy transfer-
dc.typeArticle-
dc.relation.issue2-
dc.relation.volume316-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage393-
dc.relation.lastpage397-
dc.relation.journaltitleBiochemical and Biophysical Research Communications-
dc.identifier.doi10.1016/j.bbrc.2004.02.059-
dc.identifier.wosidWOS:000220333200015-
dc.identifier.scopusid2-s2.0-1542722220-
dc.author.googleKim J.-
dc.author.googleLee M.-
dc.contributor.scopusid이민영(55582235800)-
dc.date.modifydate20180501154203-
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE