Shukla, Anshuman and Raje, Manoj and Guptasarma, Purnananda (2008) Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers. Biochemistry. Biokhimii͡a, 73 (6). pp. 681-5. ISSN 0006-2979
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Abstract
The sequence-reversed form of a small heat shock protein, HSP12.6 (retro-HSP12.6), has been reported to fold and assemble into structured tetramers in aqueous solution. Upon raising the protein concentration to ~1.0-1.5 mg/ml, tetrameric retro-HSP12.6 is known to display a tendency to associate further into spherical beads of 18-20 nm in diameter containing folded protein subunits. Here we report that storage of this protein at low temperatures leads to further association of the beaded structures into linear and ring-shaped amyloid nanofibers of 18-20 nm in diameter. The electron micrographs presented in this communication provide the best visual evidence yet that amyloids can form through the association of smaller structured bead-like intermediates. The results also suggest that folded beta-sheet-rich subunits can participate in amyloid formation.
Item Type: | Article |
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Additional Information: | Copyright of this article belongs to Springer Science |
Subjects: | Q Science > QD Chemistry |
Depositing User: | Dr. K.P.S.Sengar |
Date Deposited: | 08 Dec 2011 19:37 |
Last Modified: | 19 Jan 2015 05:35 |
URI: | http://crdd.osdd.net/open/id/eprint/585 |
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