What is it about?
This study investigates how proteins behave in crowded environments, specifically examining the role of crowder molecule size in modulating protein stability and dynamics. By using two differently sized dextrans as crowders, the researchers reveal how protein unfolding is influenced by both entropic and enthalpic contributions under these conditions.
Featured Image
Photo by Pawel Czerwinski on Unsplash
Why is it important?
Proteins inside cells face a crowded environment filled with macromolecules, and their stability can depend on the size of surrounding molecules. This work provides crucial insights into how these crowding effects operate, advancing our understanding of cellular processes and aiding the design of better biomimetic environments for protein research.
Perspectives
This paper highlights the nuanced ways in which crowding affects proteins, moving beyond the traditional view of excluded volume effects. The insights into enthalpy-entropy compensation and size-dependent interactions are particularly intriguing, offering a deeper understanding of how proteins function in real cellular environments.
Dr. Nilimesh Das
Harvard University
Read the Original
This page is a summary of: Size-dependent macromolecular crowding effect on the thermodynamics of protein unfolding revealed at the single molecular level, International Journal of Biological Macromolecules, December 2019, Elsevier,
DOI: 10.1016/j.ijbiomac.2019.09.029.
You can read the full text:
Contributors
The following have contributed to this page
