Skip to main content
. Author manuscript; available in PMC: 2015 Apr 17.
Published in final edited form as: Biochemistry. 2006 Nov 14;45(45):13670–13676. doi: 10.1021/bi061368x

Fig. 1.

Fig. 1

A. Typical thermal unfolding profiles, measured by circular dichroism at 222 nm, corrected for linear changes above and below the sigmoidal unfolding transition, of expressed single repeats of αII spectrin. The curves, from left to right, show unfolding of repeats 12, 4, 13 and 1. B. The Tm of all repeats along the αII spectrin chain. The horizontal line corresponds to physiological temperature. The scale on the right shows the approximate free energy of unfolding of the repeats at 37°C, and applies also to the β-chain repeats in panel D. C. Typical thermal unfolding profiles for single repeats of βII spectrin, corrected as above. The curves, from left to right, are show unfolding of repeats 13, 9, 12 and 10. D. The Tm of all repeats along the βII spectrin chain.