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ID: 17042.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Amyloid fibrils from the mammalian protein prothymosin α
Authors:Pavlov, N. A.; Cherny, D. I.; Heim, G.; Jovin, T. M.; Subramaniam, V.
Language:English
Date of Publication (YYYY-MM-DD):2002-04-24
Title of Journal:FEBS Letters
Volume:517
Issue / Number:1-3
Start Page:37
End Page:40
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Mammalian prothymosin α, a small (12 kDa) and extremely acidic protein (pI 3.5), is a member of the growing family of `natively' unfolded proteins. We demonstrate that at low pH ( similar to 3) and high concentrations, prothymosin α is capable of forming regular elongated fibrils with flat ribbon structure 4-5 nm in height and 12-13 nm in width as judged from scanning force and electron microscopy. These aggregates induced a characteristic spectral shift of thioflavin T fluorescence and their circular dichroism spectra were indicative of significant beta-sheet content, suggesting formation of classical amyloid. Our findings indicate that natively unfolded proteins may have a general propensity to form amyloid fibrils under conditions inducing partially folded conformations. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Free Keywords:natively unfolded; protein aggregation; amyloid fibrils; scanning force microscopy; electron microscopy
Comment of the Author/Creator:Date: 2002, APR 24
Last Change of the Resource (YYYY-MM-DD):2004-08-04
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
External Affiliations:Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Moscow 119899, Russia; Russian Acad Sci, Inst Mol Genet, Moscow 123182, Russia
Identifiers:URL:http://www.sciencedirect.com/science?_ob=MImg&_ima...
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