| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5379201 | Chemical Physics Letters | 2016 | 25 Pages |
Abstract
- Antifreeze activity is found to be correlated with a change in hydrogen bond dynamics.
- The 'hydration funnel', i.e. a retardation of hydration bond dynamics toward the ice binding site is found to be a general phenomena for antifreeze proteins.
- Cosolutes, such as sodium citrate influence the hydrogen bond dynamics and increase the antifreeze activity of the protein.
- Using THz absorption spectroscopy we can state that sodium citrate has a local, direct interaction with the protein.
- Whereas changes in the collective hydrogen bond dynamics are a necessary condition for antifreeze activity, the local mechanism determines the size of the antifreeze activity.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Yao Xu, Alexander Bäumer, Konrad Meister, Connor G. Bischak, Arthur L. DeVries, David M. Leitner, Martina Havenith,
