Fig. 4: The oligoalanine chains in complex coacervates form rigid aggregates with different secondary structures. | Communications Chemistry

Fig. 4: The oligoalanine chains in complex coacervates form rigid aggregates with different secondary structures.

From: Crosslinking, salt-induced aging, and secondary structure formation in Peptide-containing coacervates inspired by spider silk

Fig. 4

1D 13C MAS ssNMR experiments and secondary chemical shift analysis on the GPBL/pAA coacervates at [NaCl] = 0.4 M (red) and 0.1 M (blue). a 1D 13C direct excitation (DE) experiment for both GPB samples. Regions with carbon beta (Cβ), carbon alpha (Cα), and carbonyl peaks (CO) are indicated; b Deconvolution of Cβ and Cα regions; c 1D 13C cross-polarization (CP; top) and insensitive nuclei enhanced by polarization transfer (INEPT; bottom) spectra, showing rigid and mobile residues, respectively. Peaks are labeled according to the secondary structure: α-helix (αh), β-sheet (βs), and random coil (rc); contaminant and solvent peaks are marked with a star; d Bar-graph representing the percentage of secondary structure. The secondary structures are colored green for β-sheet, light blue for α-helix, and orange for random coil, as indicated. Error bars represent the standard deviation obtained from 100 Monte Carlo iterations of peak-fitting deconvolution applied to a single dataset82.

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