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. Author manuscript; available in PMC: 2016 Apr 6.
Published in final edited form as: Biochemistry. 2007 Mar 6;46(12):3624–3634. doi: 10.1021/bi061785+

Table 1.

Summary of equilibrium stability measurements for WT HP36 and its mutants in 10 mM sodium acetate, 150 mM sodium chloride, pH 5.0 at 25°C.

protein Tm (°C) Δ (Tm) (kcal mol-1) ΔU (H2O) (kcal mol-1) M (kcal mol-1 M-1)
WT HP36 73.0 31.8 3.22 -0.52
D44N 57.8 32.1 2.48 -0.55
F47L 45.6 15.8 0.52a -0.45b
R55M 67.3 26.3 2.19 -0.43
D44NR55M 55.4 27.4 1.74 -0.44
F47LR55M 35.3 9.8 0.19-0.28c N/A
a

ΔU (H2O) of F47L is extrapolated from urea denaturation in different TMAO concentrations;

b

m is the average value of the m from urea denaturation in different TMAO concentrations;

c

ΔU (H2O) of F47LR55M is calculated from Gibbs-Helmholtz equation using ΔP values ranging from 0.30-0.70 kcal mol-1 K-1.