Kinetic and thermodynamic stability properties of the hI and s5A α1AT variants.

akN→I and kI→U represent the rates for the N→I and the I→U transitions when the proteins were denatured in 4 M GdnHCl.bThe GdnHCl-induced unfolding curves were analyzed using the three-state unfolding function to determine the midpoints of the N→I transition (DmN→I) and the I→U transition (DmI→U). ΔΔGN→I represents the change in free energy for the N→I transition (all experimental errors were within ±0.12 kcal/mol) and ΔΔGI→U the change in free energy for the I→U transition (all experimental errors were within ±0.12 kcal/mol).cThe thermal denaturation curves obtained using far-UV CD were analyzed using the two-state unfolding function to determine the midpoint of transition. Each experiment was performed three times. Errors included represent the standard deviation of each dataset.