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. Author manuscript; available in PMC: 2020 May 28.
Published in final edited form as: ACS Biomater Sci Eng. 2019 Sep 24;6(5):2682–2695. doi: 10.1021/acsbiomaterials.9b01213

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%