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Recombinant Human Chaperonin 10 produced in E. coli has a molecular mass of approximately 11 KDa.
>95% as determined by SDS-PAGE.
Liquid. In Tris-HCl Buffer (pH 7.4).
A chaperonin called GroEL-GroES complex (from Escherichia coli) (PDB code=1aon). Two rings of 7x2GroEL proteins (shown in blue and green) with a cap (just on one side) of GroES proteins (red and yellow). Unfolded proteins enter that cavity (which is protein sized) to be protected during folding.
Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg-ATP facilitate refolding and reactivation of denaturedproteins. Chaperonin 10 (GroES) is expressed in E. coli.
ATP binding, chaperone binding, unfold protein binding