Table 3 Degree of structural unfolding in the transition state for the irreversible denaturation of hPGK1 variants determined by DSC.

From: Loss of stability and unfolding cooperativity in hPGK1 upon gradual structural perturbation of its N-terminal domain hydrophobic core

Variant

m≠ (kcal·mol−1·M−1)

m≠/munf

WT

2.69 ± 0.36

0.59 ± 0.08

F25L

2.47 ± 0.34

0.54 ± 0.07

F25V

2.74 ± 0.51

0.60 ± 0.11

F25A

2.60 ± 0.60

0.57 ± 0.13

F25G

1.93 ± 0.42

0.43 ± 0.09

F25W

2.63 ± 0.48

0.58 ± 0.11

  1. m≠ values were determined from DSC experiments and Eq. (5). munf is the theoretical value (4.54 kcal mol−1 M−1) for the full unfolding of the protein29 based on a protein size of 417 residues42.
Back to article page