Effect of Dextran 70 on the thermodynamic and structural properties of proteins.
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.
Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Delhi, India.
Gurumayum Suraj
GS
Sharma
Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Delhi, India.
Shruti
S
Mittal
Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Delhi, India. Electronic address: lairksingh@gmail.com.
Laishram Rajendrakumar
LR
Singh
D000818:Animals; D002417:Cattle; D002645:Chickens; D003911:Dextrans / Q000737:chemistry*; D004527:Egg Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007768:Lactalbumin / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D010179:Pancreas / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D012996:Solutions; D013816:Thermodynamics
D003911:Dextrans; D004527:Egg Proteins; D012996:Solutions; D007768:Lactalbumin; D012259:Ribonuclease, Pancreatic; D009113:Muramidase
Macromolecular crowding; Macromolecules; Protein folding