Table 3 |
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Thermodynamic parameters from GdnHCl unfolding studies of native and glycated insulin. |
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ΔGo(H2O) (kcal·mol-1) |
m (kcal·mol-1.M-1) |
Cm (M) |
|
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|
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Insulin |
3.34 ± 0.33 |
0.63 ± 0.10 |
5.31 ± 0.98 |
|
Glycated Insulin |
2.66 ± 0.27 |
0.52 ± 0.09 |
5.10 ± 0.98 |
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|
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Parameters were obtained by a direct fit of the model equations to experimental data in Figure 4 D and E. ΔGo(H2O) is the protein conformational stability; m is the dependence of ΔGoon denaturant concentration; Cm is the denaturant concentration at the midpoint of the unfolding transition. |
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Oliveira et al. BMC Biochemistry 2011 12:41 doi:10.1186/1471-2091-12-41 |
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