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. Author manuscript; available in PMC: 2012 Feb 11.

Published in final edited form as: J Mol Biol. 2010 Nov 25;406(1):75–91. doi: 10.1016/j.jmb.2010.11.031

Fig. 2 — Circular dichroism (CD) of caspase-6 cleavage variants. (a) Thermal denaturation profiles of caspase-6 cleavage variants unliganded (apo) or with the active-site ligand VEID in physiological (120 mM) or high (500 mM) NaCl concentrations. The measured T_m did not vary between runs, however run-to-run variation in the shape and slope of the pre-melt transition precluded meaningful interpretation of this region of the melting curve. (b) CD spectra of caspase-6 cleavage variants at 12°C (black) or 90°C (gray). The [θ]₂₀₈/[θ]₂₂₂ values at 12°C are indicated above each spectra. Each variant was measured using two independently prepared and concentrated samples on two different days. The spectral features were observed in duplicate spectra and a representative spectrum for each variant is shown. NA Not applicable due to inability to functionally verify binding of VEID to the active site. ND Not Detectable.

Fig. 2 — Circular dichroism (CD) of caspase-6 cleavage variants. (a) Thermal denaturation profiles of caspase-6 cleavage variants unliganded (apo) or with the active-site ligand VEID in physiological (120 mM) or high (500 mM) NaCl concentrations. The measured T_m did not vary between runs, however run-to-run variation in the shape and slope of the pre-melt transition precluded meaningful interpretation of this region of the melting curve. (b) CD spectra of caspase-6 cleavage variants at 12°C (black) or 90°C (gray). The [θ]₂₀₈/[θ]₂₂₂ values at 12°C are indicated above each spectra. Each variant was measured using two independently prepared and concentrated samples on two different days. The spectral features were observed in duplicate spectra and a representative spectrum for each variant is shown. NA Not applicable due to inability to functionally verify binding of VEID to the active site. ND Not Detectable.