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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Effect of Dextran 70 on the thermodynamic and structural properties of proteins
Gurumayum Suraj Sharma1, Shruti Mittal1, Laishram Rajendrakumar Singh1
1Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Delhi, India.
Abstract:
Biological macromolecules are known to evolve and function under crowded intracellular environments that comprises of a wealth of soluble and insoluble macromolecules like proteins, nucleic acids, ribosomes and carbohydrates etc. Crowded environment is known to result in altered biological properties including thermodynamic, structural and functional aspect of macromolecules as compared to the macromolecules present in our commonly used experimental dilute buffers. In this study, we have investigated the effect of Dextran 70 on the thermodynamic and structural properties of three different proteins (Ribonuclease-A, lysozyme and holo α-lactalbumin) at different pH values. We discovered that Dextran 70 has a protein-independent effect in terms of protein stability and structure.
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