Abstract
The majority of pKa values in protein unfolded states are close to the amino acid model pKa values, thus reflecting the weak intramolecular interactions present in the unfolded ensemble of most proteins. We have carried out thermal denaturation measurements on the WT and eight mutants of HEWL from pH 1.5 to pH 11.0 to examine the unfolded state pKa values and the pH dependence of protein stability for this enzyme. The availability of accurate pKa values for the folded state of HEWL and separate measurements of mutant-induced effects on the folded state pKa values, allows us to estimate the pKa values of seven acidic residues in the unfolded state of HEWL. Asp-48 and Asp-66 display pKa values of 2.9 and 3.1 in our analysis, thus representing the most depressed unfolded state pKa values observed to date. We observe a strong correlation between the folded state pKa values and the unfolded state pKa values of HEWL, thus suggesting that the unfolded state of HEWL possesses a large degree of native state characteristics.
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