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Table 3 Thermodynamic parameters from GdnHCl unfolding studies of native and glycated insulin.

From: Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formation

 

ΔGo(H2O)

(kcal·mol-1)

m

(kcal·mol-1.M-1)

Cm

(M)

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

  1. 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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BMC Biochemistry

ISSN: 1471-2091

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