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. Author manuscript; available in PMC: 2010 Aug 4.
Published in final edited form as: Biochemistry. 2009 Aug 4;48(30):7334–7341. doi: 10.1021/bi900467a

Table 3.

Thermal denaturation parameters of wild type and mutant HγS-crystallin

protein ΔSma ΔHm(kcal/mol)b Tmc ΔTmd Δ(ΔG)e
WT (Fl Ratio curve) 0.462±0.014 161.057±4.940 75.56±0.15
MUT (Fl Ratio curve) 0.099 ± 0.001 33.231±0.379 61.49±0.17 -14.07 -6.498
 N↔I
MUT (Fl Ratio curve) 0.318±0.012 108.963±4.064 69.45±0.25 -6.11 -2.822
 I↔U
WT (CD curve) 0.440±0.018 153.2±6.269 75.05±0.16
MUT(CD curve) 0.219±0.036 74.2±12.192 65.46±0.15 -9.59 -4.219
a

slope of ΔG versus T at Tm in Kcal/mol/deg.

b

ΔHm=[Tm(K)]×( ΔSm) in Kcal/mol.

c

midpoint of thermal unfolding curve in °C.

d

difference between the Tm values.

e

Δ(ΔG)= ΔTm ×ΔSm. where ΔSm is value for the wild type protein.