Related Experiment Video
Updated: Jun 28, 2026

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Crystal structure and assembly of a eukaryotic small heat shock protein
R L van Montfort1, E Basha, K L Friedrich
1Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX UK.
Abstract:
The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation.
More Related Videos
Related Concept Videos
Protein Organization
Protein Folding
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Molecular Chaperones and Protein Folding
The...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Bacterial Protein Maturation

