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Palmitoylation facilitates folding of IFG1R JM analogs. (A) CD spectra of a non-palmitoylated analog of 16, 28 (Ac-RNNSRLGNGVLY-NH2) reveals unordered structure both in water and in dodecylphosphocholine micelles. (B) CD spectra of 16 (Pal-RNNSRLGNGVLY-NH2) reveal significant differences in peptide fold in dodecylphosphocholine micelles compared to water. Compound 22, the retro-inverso version of 16, had a stronger CD signal.
