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Effect of Dextran 70 on the thermodynamic and structural properties of proteins.

Authors :
Sharma GS
Mittal S
Singh LR
Source :
International journal of biological macromolecules [Int J Biol Macromol] 2015 Aug; Vol. 79, pp. 86-94. Date of Electronic Publication: 2015 Apr 29.
Publication Year :
2015

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.<br /> (Copyright © 2015. Published by Elsevier B.V.)

Details

Language :
English
ISSN :
1879-0003
Volume :
79
Database :
MEDLINE
Journal :
International journal of biological macromolecules
Publication Type :
Academic Journal
Accession number :
25936502
Full Text :
https://doi.org/10.1016/j.ijbiomac.2015.04.051