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. Author manuscript; available in PMC: 2008 Dec 8.
Published in final edited form as: Biochemistry. 2007 Jul 7;46(30):8861–8871. doi: 10.1021/bi700487q

Table 3.

Apparent Free Energy of unfolding for WT, Q85E, Q180E, and Q85E/Q180E βA3-crystallin.

Protein a CM bΔCM c Apparent ΔGD0 d Apparent ΔΔGD0
WTβA3 4.5 ±< 0.1 14 ± 2.0
Q85E 4.2 ±< 0.1 −0.3 ±< 0.1 10 ±0.1 −4.0 ±2.1
Q180E 4.1 ±< 0.1 −0.4 ±< 0.1 9.6 ± 0.8 −4.4 ± 1.9
Q85E/Q180E 3.7 ±< 0.1 −0.8 ±< 0.1 4.4 ± 0.4 −9.6 ± 2.4
a

The midpoints of unfolding transitions for mutants from extrapolation method.

b

ΔCM=CMmutant-CMwildtype in units of M.

c

The Apparent ΔG 0 (kcal/mol), of unfolding based on urea curves. RT1nK values were calculated for K =fD/fN from the transition region of the urea denaturation curves.

d

Apparent ΔΔGD0=ΔGD0mutant-ΔGD0wild type in units of kcal/mol.