Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 이민영 | - |
dc.date.accessioned | 2018-05-02T08:15:49Z | - |
dc.date.available | 2018-05-02T08:15:49Z | - |
dc.date.issued | 2004 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.other | OAK-2074 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/242817 | - |
dc.description.abstract | We 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.language | English | - |
dc.title | Observation of multi-step conformation switching in β-amyloid peptide aggregation by fluorescence resonance energy transfer | - |
dc.type | Article | - |
dc.relation.issue | 2 | - |
dc.relation.volume | 316 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.startpage | 393 | - |
dc.relation.lastpage | 397 | - |
dc.relation.journaltitle | Biochemical and Biophysical Research Communications | - |
dc.identifier.doi | 10.1016/j.bbrc.2004.02.059 | - |
dc.identifier.wosid | WOS:000220333200015 | - |
dc.identifier.scopusid | 2-s2.0-1542722220 | - |
dc.author.google | Kim J. | - |
dc.author.google | Lee M. | - |
dc.contributor.scopusid | 이민영(55582235800) | - |
dc.date.modifydate | 20190901081003 | - |