Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/46200
DC FieldValueLanguage
dc.contributor.authorSrisailam, S.en_US
dc.contributor.author詹富智zh_TW
dc.contributor.authorKrishnaswamy, T.en_US
dc.contributor.authorKumar, T.K.S.en_US
dc.contributor.authorRajalingam, D.en_US
dc.contributor.authorKathir, K.M.en_US
dc.contributor.authorSheu, H.S.en_US
dc.contributor.authorJan, F.J.en_US
dc.contributor.authorChao, P.C.en_US
dc.contributor.authorYu, C.en_US
dc.date2003zh_TW
dc.date.accessioned2014-06-06T08:18:54Z-
dc.date.available2014-06-06T08:18:54Z-
dc.identifier.issn0021-9258zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/46200-
dc.description.abstractAcidic fibroblast growth factor from newt (Notopthalmus viridescens) is a similar to15-kDa, all beta-sheet protein devoid of disulfide bonds. In the present study, we investigate the effects of 2,2,2-trifluoroethanol (TFE) on the structure of newt acidic fibroblast growth factor (nFGF-1). The protein aggregates maximally in 10% (v/v) TFE. Congo red and thioflavin T binding experiments suggest that the aggregates induced by TFE have properties resembling the amyloid fibrils. Transmission electron microscopy and x-ray fiber diffraction data show that the fibrils (induced by TFE) are straight, unbranched, and have a cross-beta structure with an average diameter of 10-15 Angstrom. Preformed fibrils (induced by TFE) of nFGF-1 are observed to seed amyloid-like fibril formation in solutions containing the protein (nFGF-1) in the native beta-barrel conformation. Fluorescence, far-UV CD, anilino-8-napthalene sulfonate binding, multidimensional NMR, and Fourier transformed infrared spectroscopy data reveal that formation of a partially structured intermediate state(s) precedes the onset of the fibrillation process. The native beta-barrel structure of nFGF-1 appears to be disrupted in the partially structured intermediate state(s). The protein in the partially structured intermediate state(s) is found to be "sticky" with a solvent-exposed non-polar surface(s). Amyloid fibril formation appears to occur due to coalescence of the protein in the partially structured intermediate state(s) through solvent-exposed non-polar surfaces and intermolecular beta-sheet formation among the extended, linear beta-strands in the protein.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Biological Chemistryen_US
dc.relation.ispartofseriesJournal of Biological Chemistry, Volume 278, Issue 20, Page(s) 17701-17709.en_US
dc.relation.urihttp://dx.doi.org/10.1074/jbc.M300336200en_US
dc.subjectfibroblast-growth-factoren_US
dc.subjectalpha-synucleinen_US
dc.subjectelectron-microscopyen_US
dc.subjectparkinsons-diseaseen_US
dc.subjectglobular-proteinen_US
dc.subjecthuman lysozymeen_US
dc.subjectin-vitroen_US
dc.subjectaggregationen_US
dc.subjectprionen_US
dc.subjectinsulinen_US
dc.titleAmyloid-like fibril formation in an all beta-barrel protein - Partially structured intermediate state(s) is a precursor for fibril formationen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1074/jbc.M300336200zh_TW
item.languageiso639-1en_US-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextno fulltext-
Appears in Collections:植物病理學系
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