GroEL peptide substrates

Figure 7.35 GroEL peptide substrates (a) Basic Amphiphilic (Bamph) peptide, the optimal first round substrate peptide. Hydrophilic residues (red) and hydrophobic residues (green) are disposed for B h to have the ability to form an amphiphilic a-helix in solution (left), considered to be potentially optfmal to interact with exposed hydrophobic residue "patches" in GroEL (coloured regions in GroEL monomer riahti (b) Summary of AMPH and NON-AMPH series peptides with helix forming template (Ro 47-1615) and control template (Ro 47-1614) (right) and proposed amphiphilic (AMPH) (upper left) and non-amphiphilic (NON-AMPH) helical structures (lower left) illustrated (peptide structure illustrations in a) and b) are adapted from Preuss et al., 1999, Fig. 3).

Seven GroES, 10,000 Da protein molecules, bind coincident with ATP binding at one end of the D7 GroEL structure to cap the structure and enclose a water-filled cavity of 175,000 A with the capacity to contain protein or peptide substrate inside of a size up to 70kDa. 

---