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. Author manuscript; available in PMC: 2012 Mar 9.
Published in final edited form as: Structure. 2011 Mar 9;19(3):349–360. doi: 10.1016/j.str.2010.12.018

Figure 5. Temperature dependence of consensus ankyrin repeat unfolding.

Figure 5

(A) Thermal denaturation of CARPs in varying amounts of guanidine hydrochloride (see legend). (B) GdnHCl titrations at different temperatures. Lines result from global fits, with mi,i+1/mi=0.5. For each construct (legend) there are eight GdnHCl titrations performed at 5, 10, 15, 20, 25, 30, 35 and 40°C (increasing color from 5 to 40°C). (C) Three dimensional representation of the temperature and GdnHCl dependence of CARP folding. Curves in (A) and (B) and surfaces in (C) result global Ising analysis as a function of temperature and GdnHCl, with mi,i+1/mi=0.5. Surfaces in (C) are, from left to right, NR2, NR2C, R3C, NR3, NR3C, R4C, NR4. Conditions: 150mM NaCl, 25 mM NaOAc, pH 5.0. To compare reversibility and structure at pH 8.0 and 5.0, see Figure S3.