TY  - JOUR
N1  - Copyright of this article belongs to Springer Science
ID  - open585
UR  - http://www.springerlink.com/content/w382746300qgvx41/fulltext.pdf
IS  - 6
A1  - Shukla, Anshuman
A1  - Raje, Manoj
A1  - Guptasarma, Purnananda
Y1  - 2008/06//
N2  - 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.
PB  - Springer Science
JF  - Biochemistry. Biokhimii?a
VL  - 73
SN  - 0006-2979
TI  - Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers.
SP  - 681
AV  - restricted
EP  - 5
ER  -