title: Supramolecular structure of the recombinant murine small heat shock protein hsp25.
abstract: The size and shape of the recombinant murine small heat shock protein, hsp25, have been analyzed by hydrodynamic and electron microscopic methods. According to these studies recombinant hsp25 exists in large complexes with a sphere-like shape and diameters of 15-18 nm. The molecular mass of these complexes amounts to about 730 kDa indicating that they are composed of about 32 monomers.
authors.affiliation: Institute of Molecular Biology, Berlin, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Behlke
authors.forename: G
authors.initials: G
authors.lastname: Lutsch
authors.forename: M
authors.initials: M
authors.lastname: Gaestel
authors.forename: H
authors.initials: H
authors.lastname: Bielka
mesh_terms: D000818:Animals; D006360:Heat-Shock Proteins / Q000737:chemistry*; D046911:Macromolecular Substances; D051379:Mice; D008854:Microscopy, Electron; D008958:Models, Molecular; D009363:Neoplasm Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D014461:Ultracentrifugation
chemical_list: D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D009363:Neoplasm Proteins; D011994:Recombinant Proteins