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

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers.
 
Creator Shukla, Anshuman
Raje, Manoj
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
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/585/1/guptasarma08.17.pdf
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://www.springerlink.com/content/w382746300qgvx41/fulltext.pdf
http://crdd.osdd.net/open/585/