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. Author manuscript; available in PMC: 2018 Mar 31.
Published in final edited form as: Biochem J. 2018 Mar 29;475(6):1177–1196. doi: 10.1042/BCJ20170913

Figure 5. The CARD and core of caspase-9 unfold as a single unit when the intersubunit linker is intact.

Figure 5

Thermal denaturation profiles monitored by circular dichroism (left) with the thermal melting temperatures (Tm) for each transition listed and circular dichroism spectra (right) of various forms of caspase-9.

(A) Monomeric, zymogen (uncleaved) caspase-9 (catalytic site-inactivated C287A) exhibited a single melting transition, which suggests cooperative unfolding of CARD and core of caspase-9.

(B) Cleavage of the linker of (A) by caspase-3 results in independent unfolding, as manifested by two separate melting transitions.

(C) Zymogen (catalytic site-inactivated C287A), uncleaved caspase-9 in a constitutively dimeric state (cDimer) shows a single melting transition.

Plots are representative of three trials. Tm values shown are means ± SEM of three trials done on three separated days.