Table 1: Chou-Fasman secondary structure predictions from amino acid sequences for the bifunctional peptide and its constitutive domains.
Secondary structure features including helix (α, 310 and π-helix), beta (β-bridge, bonded turn), and irregular (bend and loop) features.
α-helix | β-strand | irregular | |
---|---|---|---|
TiBP | 0% | 0% | 100% |
AMPA | 60% | 0% | 40% |
GL13K | 0% | 0% | 100% |
TiBP-AMPA | 69% | 0% | 31% |
TiBP-GL13K | 50% | 0% | 50% |