Unformatted text preview: /‘\ Mechanism for Hsp70 induced folding
Hsp70 prevents ‘incorrect’ early folded structures 70/40 bind to hydrophobic patches (some specificity) Allows entire protein to be made before ‘controlled’
fold. How does it control folding?
Cycles of fold/unfold? GroEL/GroES chaperone system Gro EL -Oligomer of 60 kD protein (Hsp60) 14 subunits — 2 heptamer rings Gro ES —- Heptamer dome — of 10 kD protein (Hsp10)
Total MW. ~ 106 amu. Refolds ~15% of E coli polypeptides Polypeptides cannot be too big ...
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- Fall '09