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- W2910197057 abstract "Although a protein's stability derives from its structure, ligands can also affect structure and stability. The bacterial copper chaperone CusF is stabilized via ligand binding of silver or copper ion, showing increased stability to thermal and chemical denaturation. We are investigating the thermodynamic mechanism of this stabilization through tryptophan fluorescence measurements of CusF unfolding behavior in the absence (apo) and presence (holo) of its ligand Ag(I). Stability curve analysis shows the temperature- and ligand dependence of enthalpy, entropy, and heat capacity of unfolding. We show that ligand binding increases CusF's unfolding enthalpy (ΔH) by approximately 5kcal-mol, its heat capacity (ΔCp) by 0.5kcal-mol, and its entropy (ΔS) by 30 cal-mol. Though the enthalpy change is the most obvious determinant of CusF's ligand-dependent stabilization, the mixed mechanism - particularly the heat capacity change - leaves open the possibility that CusF might show residual structure in the unfolded state of its holo-structure. Such residual structure would narrow the difference between folded and unfolded state heat capacities, resulting in a smaller ΔCp and a wider range of apparent thermal stability." @default.
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- W2910197057 date "2019-02-01" @default.
- W2910197057 modified "2023-09-30" @default.
- W2910197057 title "Measuring the Unfolding and Ligand-Binding of CusF, a Copper Chaperone" @default.
- W2910197057 doi "https://doi.org/10.1016/j.bpj.2018.11.1833" @default.
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