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. 2018 Jun 7;293(28):10895–10910. doi: 10.1074/jbc.RA118.003650

Table 2.

Thermodynamic stabilities of insulin analogs

Analog ΔGua Cmid mb
kcal mol1 m kcal mol1 m1
Wildtype 3.4 ± 0.1c 5.0 ± 0.1 0.68 ± 0.02
OrnB29 3.3 ± 0.1 4.9 ± 0.1 0.67 ± 0.01
TrpB26,OrnB29 3.3 ± 0.1 5.1 ± 0.2 0.64 ± 0.03

a Parameters were inferred from CD-detected guanidine denaturation data by application of a two-state model; uncertainties represent fitting errors for a given data set.

b The m-value (slope Δ(G)/Δ(M)) correlates with surface area exposed on denaturation.

c Analysis of replicates of [TrpB26,OrnB29]insulin, parent [OrnB29]insulin, and WT samples indicated that experimental standard errors were equal to or less than the above fitting errors: ±0.1 kcal mol−1Gu), ±0.1 m (Cmid), and ±0.01 kcal mol−1 m−1 (m).