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Amyloid fibrils from the mammalian protein prothymosin α

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Pavlov,  N. A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Cherny,  D. I.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Heim,  G.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

Jovin,  T. M.
Max Planck Society;

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Subramaniam,  V.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F3F7-6
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.