Browsing Meister, Konrad by Title
Now showing items 7-8 of 8
Specific Ion–Protein Interactions Influence Bacterial Ice NucleationIce nucleation-active bacteria are the most efficient ice nucleators known, enabling the crystallization of water at temperatures close to 0 °C, thereby overcoming the kinetically hindered phase transition process at these conditions. Using highly specialized ice-nucleating proteins (INPs), they can cause frost damage to plants and influence the formation of clouds and precipitation in the atmosphere. In nature, the bacteria are usually found in aqueous environments containing ions. The impact of ions on bacterial ice nucleation efficiency, however, has remained elusive. Here, we demonstrate that ions can profoundly influence the efficiency of bacterial ice nucleators in a manner that follows the Hofmeister series. Weakly hydrated ions inhibit bacterial ice nucleation whereas strongly hydrated ions apparently facilitate ice nucleation. Surface-specific sum-frequency generation spectroscopy and molecular dynamics simulations reveal that the different effects are due to specific interactions of the ions with the INPs on the surface of the bacteria. Our results demonstrate that heterogeneous ice nucleation facilitated by bacteria strongly depends upon the nature of the ions, and specific ion–protein interactions are essential for the complete description of heterogeneous ice nucleation by bacteria.
Toward Understanding Bacterial Ice NucleationBacterial ice nucleators (INs) are among the most effective ice nucleators known and are relevant for freezing processes in agriculture, the atmosphere, and the biosphere. Their ability to facilitate ice formation is due to specialized ice-nucleating proteins (INPs) anchored to the outer bacterial cell membrane, enabling the crystallization of water at temperatures up to −2 °C. In this Perspective, we highlight the importance of functional aggregation of INPs for the exceptionally high ice nucleation activity of bacterial ice nucleators. We emphasize that the bacterial cell membrane, as well as environmental conditions, is crucial for a precise functional INP aggregation. Interdisciplinary approaches combining high-throughput droplet freezing assays with advanced physicochemical tools and protein biochemistry are needed to link changes in protein structure or protein–water interactions with changes on the functional level.