TABLE 2.
Secondary structure predictions of chaperonin peptidesa
| Protein | Position and sequence |
|---|---|
| Cpn 60.1 | 195 KGFLSAYFVTDFDNQQAVLEDALIL 219 |
| EEEEEE HHHHHHHHHH | |
| Cpn 60.2 | 195 KGYISGYFVTDPERQEAVLEDPYIL 219 |
| EEEEEE HHHHHHH | |
| GroEL | 197 RGYLSPYFINKPETGAVELESPFIL 221 |
| E EEEE | |
| IIBIBISBXXXXXSBXBXBXXBXBB |
a
E, β-sheet; H, α-helix; I, exposed to internal cavity; B, buried; S, intersubunit contact; X, exterior exposure. The table shows an alignment of the peptide sequences tested for the simulation of cytokine secretion. The secondary structures were predicted using the consensus method Jpred (7) via the server at http://jpred.ebi.ac.uk/ and are listed under each sequence. The environments of each amino acid side chain (I, B, S, and X) in the GroEL structure (25) are listed in the bottom row.