title: Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers.
creator: Shukla, Anshuman
creator: Raje, Manoj
creator: Guptasarma, Purnananda
subject: QD Chemistry
description: 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.
publisher: Springer Science
date: 2008-06
type: Article
type: PeerReviewed
format: application/pdf
identifier: http://crdd.osdd.net/open/585/1/guptasarma08.17.pdf
relation: http://www.springerlink.com/content/w382746300qgvx41/fulltext.pdf
identifier:   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     
relation: http://crdd.osdd.net/open/585/