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Updated: Aug 6, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Comment on "Aggregation Interface and Rigid Spots Sustain the Stable Framework of a Thermophilic N-Demethylase"
Daniel M Wade1, Walker S Lewis1, Jonghoon Kang1
1Department of Biology, Valdosta State University, Valdosta, Georgia 31698, United States.
Abstract:
The thermal properties of proteins are very important in industrial, agricultural, and food chemistry. A recent article (Li, B., et al. J. Agric. Food Chem. 2023, 71, 5614-5629) examines the thermal denaturation of enzymes TrSOX and BSOX by measuring the enthalpy change and melting temperature in the denaturation. In this work, we report the numerical values of entropy in the denaturation of proteins and show that both proteins TrSOX and BSOX exhibit enthalpy-entropy compensation in thermal denaturation, which results in a limited variation of melting temperature in both proteins. Our analysis may serve to improve our understanding of thermal properties in proteins in food chemistry.
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