Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 13, Issue 6, Pages 2294-2299Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0cp01705a
Keywords
-
Funding
- Unilever
Ask authors/readers for more resources
To help understand how sugar interactions with proteins stabilise biomolecular structures, we compare the three main hypotheses for the phenomenon with the results of long molecular dynamics simulations on lysozyme in aqueous trehalose solution (0.75 M). We show that the water replacement and water entrapment hypotheses need not be mutually exclusive, because the trehalose molecules assemble in distinctive clusters on the surface of the protein. The flexibility of the protein backbone is reduced under the sugar patches supporting earlier findings that link reduced flexibility of the protein with its higher stability. The results explain the apparent contradiction between different experimental and theoretical results for trehalose effects on proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available