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. 2012 Aug 6;287(41):34120–34133. doi: 10.1074/jbc.M112.359067

FIGURE 2.

FIGURE 2.

Shown are circular dichroism spectra of d-LAK120-A (A) in 5 mm Tris buffer solution, pH 7. 3 titrated with increasing concentrations of phosphate buffer at 37 °C. The changes in left-handed α-helix content as monitored by the ellipticity at 220 nm are shown as a function of phosphate concentration (B) and compared with corresponding experiments performed with a further four peptides. The shift in the tryptophan emission maximum (C) and the retention times on a size exclusion column (D) were also evaluated as a function of phosphate concentration and are related to the buildup of secondary structure. Lines are to guide the eye. deg, degrees. Error bars are the standard deviation of two independently repeated experiments.