Understanding Bacterial Ice Nucleation
- 1Molarcular Spectroscopy Group, MPI for Polymer Research, Mainz, Germany
- 2Multiphase Chemistry, MPI for Chemistry, Mainz, Germany
- 3Arts and Science, University of Alaska Southeast, Juneau, USA
Bacterial ice-nucleating proteins (INPs) promote heterogeneous ice nucleation better than any known material. On the molecular scale, bacterial INPs are believed to function by organizing water into ice‑like patterns to enable the formation of embryonic crystals. However, the details of their working mechanism remains largely elusive. Here, we report the results of comprehensive evaluations of environmentally relevant effects such as changes in pH, the presence of ions and temperature on the activity, three-dimensional structure and hydration shell of bacterial ice nucleators using ice affinity purification, high-throughput ice nucleation assays and surface-specific sum-frequency generation spectroscopy.
[1] Lukas, Max, et al. "Electrostatic Interactions Control the Functionality of Bacterial Ice Nucleators." Journal of the American Chemical Society 142.15 (2020): 6842-6846.
[2] Lukas, Max, et al. "Interfacial Water Ordering Is Insufficient to Explain Ice-Nucleating Protein Activity." The Journal of Physical Chemistry Letters 12 (2020): 218-223.
How to cite: Schwidetzky, R., Lukas, M., Kunert, A. T., Pöschl, U., Fröhlich-Nowoisky, J., Bonn, M., and Meister, K.: Understanding Bacterial Ice Nucleation, EGU General Assembly 2021, online, 19–30 Apr 2021, EGU21-5614, https://doi.org/10.5194/egusphere-egu21-5614, 2021.
