Fig. 5: 1D and 2D 13C MAS ssNMR experiments on the GPBL/pAA coacervate at 0.4 M NaCl. | Communications Chemistry

Fig. 5: 1D and 2D 13C MAS ssNMR experiments on the GPBL/pAA coacervate at 0.4 M NaCl.

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

Fig. 5

a 1D 13C ssNMR spectrum of the 2D CP-based experiment that shows rigid residues. b 1D 13C ssNMR spectrum of the 2D INEPT experiment, showing flexible residues. c 2D 13C-13C CP-based ssNMR experiment with 25 ms mixing time, showing rigid residues. Dotted lines show the intra-residue network of Cβ, Cα, and CO peaks of conformer βs1; d 2D 13C-13C INEPT-TOBSY ssNMR experiment showing mobile residues. Dotted lines show the intra-residue connection for rc1; e Spectral enlargement and overlay of the Cα region (black box in 2D spectra).

Back to article page