Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers.

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
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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