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. 2019 Sep 24;39(9):BSR20192196. doi: 10.1042/BSR20192196

Figure 2. CD spectra of the various peptides and trimer–peptide complexes.

Figure 2

(A) CD spectra of C34 (left) and trimer C34 (right panel). (B) CD spectra of N36 (left panel) and trimer N36 (right). Peptides were used at 50 μM, and trimers at 5 μm in 10 mM sodium phosphate buffer pH 7.4, 50 mM potassium fluoride pH 7.4. (C,D) CD spectra of peptides in an equimolar mixture: monomer N36 + trimer C34 (C) and trimer N36 + monomer C34 (D). Spectra were obtained in aqueous solution. The apparition of a maximum at 192 nm and a double minimum at 208 and 222 nm were used as indicators of peptide interactions and of the formation of an α-helical structure.