Figure 2.
Figure 2. Glycine substitution in IS6-AID linker disrupts helical structure. (A) Mean residue ellipticity at 222 nm for IS6-AID linker peptide, and AAA and GGG mutant peptides as a function of TFE concentration. Peptide sequence is shown. Black highlights the site of the GGG and AAA mutations. (B) IS6-AID linker peptide CD spectra at a peptide concentration of 50 µM in 50% TFE.

Glycine substitution in IS6-AID linker disrupts helical structure. (A) Mean residue ellipticity at 222 nm for IS6-AID linker peptide, and AAA and GGG mutant peptides as a function of TFE concentration. Peptide sequence is shown. Black highlights the site of the GGG and AAA mutations. (B) IS6-AID linker peptide CD spectra at a peptide concentration of 50 µM in 50% TFE.

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