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  Amyloid fibrils from the mammalian protein prothymosin α

Pavlov, N. A., Cherny, D. I., Heim, G., Jovin, T. M., & Subramaniam, V. (2002). Amyloid fibrils from the mammalian protein prothymosin α. FEBS Letters, 517(1-3), 37-40. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-45CDM59-6-9&_cdi=4938&_user=38661&_pii=S0014579302025723&_origin=search&_coverDate=04%2F24%2F2002&_sk=994829998&view=c&wchp=dGLbVzW-zSkzk&md5=ded5a4ccdd896ab5e687ba4159946508&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F3F7-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E57F-6
Genre: Journal Article

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 Creators:
Pavlov, N. A.1, Author              
Cherny, D. I.1, Author              
Heim, G.2, Author              
Jovin, T. M.3, Author
Subramaniam, V.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
3Max Planck Society, ou_persistent13              

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Free keywords: natively unfolded; protein aggregation; amyloid fibrils; scanning force microscopy; electron microscopy
 Abstract: 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.

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Language(s): eng - English
 Dates: 2004-08-042002-04-24
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 517 (1-3) Sequence Number: - Start / End Page: 37 - 40 Identifier: -