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. Author manuscript; available in PMC: 2009 Mar 1.

Published in final edited form as: Arch Biochem Biophys. 2007 Dec 10;471(1):32–41. doi: 10.1016/j.abb.2007.12.001

Circular dichroism spectra of apoBioB, 2Fe-BioB, and 2Fe4Fe-BioB. (A) Circular dichroism spectra of 2Fe4Fe-BioB (), 2Fe-BioB (), and apoBioB () in 10 mM MOPS, 25 mM NaF, pH 7.5 at 25 °C. The spectrum of apoBioB is also shown at 4 °C () and 95 °C () (B) Thermal unfolding of 2Fe4Fe-BioB ( ▲ ), 2Fe-BioB ( ■ ), and apoBioB ( ● ) as monitored by circular dichroism at 220 nm. Each protein was incubated at 4 °C for 6 min, a spectral reading was taken, and the temperature was raised by 2 °C, repeating up to 98 °C. Attempts to measure a comparable curve for refolding during cooling proved unsuccessful due to aggregation of the unfolded protein. Data are fit to the Gibbs-Helmholtz equation as described in Materials and Methods.

Circular dichroism spectra of apoBioB, 2Fe-BioB, and 2Fe4Fe-BioB. (A) Circular dichroism spectra of 2Fe4Fe-BioB (), 2Fe-BioB (), and apoBioB () in 10 mM MOPS, 25 mM NaF, pH 7.5 at 25 °C. The spectrum of apoBioB is also shown at 4 °C () and 95 °C () (B) Thermal unfolding of 2Fe4Fe-BioB ( ▲ ), 2Fe-BioB ( ■ ), and apoBioB ( ● ) as monitored by circular dichroism at 220 nm. Each protein was incubated at 4 °C for 6 min, a spectral reading was taken, and the temperature was raised by 2 °C, repeating up to 98 °C. Attempts to measure a comparable curve for refolding during cooling proved unsuccessful due to aggregation of the unfolded protein. Data are fit to the Gibbs-Helmholtz equation as described in Materials and Methods.