ArticleProtein science : a publication of the Protein Society2023
Characterization of the pH-dependent protein stability of 3α-hydroxysteroid dehydrogenase/carbonyl reductase by differential scanning fluorimetry.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 4 citations in OpenAlex.
- Deciphering the Function and Structure of PA1216 as an S-Adenosyl-l-Methionine Binding Protein Using Differential Scanning Fluorimetry and Circular Dichroism.Protein science : a publication of the Protein Society · 2026Article
- Hydrophobic interactions of a substrate with L193 on the flexible substrate-binding loop contribute to 3α-hydroxysteroid dehydrogenase/carbonyl reductase catalytic efficiency.Protein science : a publication of the Protein Society · 2026Article
- Measuring the Thermal Unfolding of Lysozyme: A Critical Comparison of Differential Scanning Fluorimetry and Differential Scanning Calorimetry.ChemistryOpen · 2025Article
- Characterization of the pH-dependent protein stability of 3α-hydroxysteroid dehydrogenase/carbonyl reductase by differential scanning fluorimetry.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The characterization of protein stability is essential for understanding the functions of proteins. Hydroxysteroid dehydrogenase is involved in the biosynthesis of steroid hormones and the detoxification of xenobiotic carbonyl compounds. However, the stability of hydroxysteroid dehydrogenases has not yet been characterized in detail. Here, we determined the changes in Gibbs free energy, enthalpy, entropy, and heat capacity of unfolding for 3α-hydroxysteroid dehydrogenase/carbonyl reductase (3α-HSD/CR) by varying the pH and urea concentration through differential scanning fluorimetry and presented pH-dependent protein stability as a function of temperature. 3α-HSD/CR shows the maximum stability of 30.79 kJ mol
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