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. Author manuscript; available in PMC: 2015 Jul 1.

Published in final edited form as: Prog Biophys Mol Biol. 2014 Mar 6;115(1):21–31. doi: 10.1016/j.pbiomolbio.2014.02.004

Table 1.

Stability of β-crystallins with deamidations at the domain interfaces.

βB1^a		βA3^b			βB2^c

C_M^d			C_M	ΔG_D°^e		C_M	ΔG_D1°^f	ΔG_D2°^g
Wild-type	5.9	Wild-type	4.5	14	Wild-type	2.3	7	8
		Q85E	4.2	10	Q70E	1.8	3	4
Q204E	4.1	Q180E	4.1	10	Q162E	1.8	3	8
		Q85E/Q180E	3.7	4	Q85E/Q180E	1.3	4	5

^a

Kim et al., 2002.

^b

Takata et al., 2007.

^c

Lampi et al., 2006.

^d

The molarity of urea at midpoints of apparent equilibrium transitions during unfolding.

^e

Apparent Gibbs free energy, G_D° (kcal/mol), from urea unfolding curves.

^f

Native to intermediate transition.

^g

Intermediate to unfolded transition.