TY - JOUR
T1 - Toward Understanding Bacterial Ice Nucleation
AU - Lukas, Max
AU - Schwidetzky, Ralph
AU - Eufemio, Rosemary J.
AU - Bonn, Mischa
AU - Meister, Konrad
N1 - Publisher Copyright:
© 2022 The Authors. Published by American Chemical Society.
PY - 2022/3/10
Y1 - 2022/3/10
N2 - Bacterial 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.
AB - Bacterial 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.
UR - http://www.scopus.com/inward/record.url?scp=85124160144&partnerID=8YFLogxK
U2 - 10.1021/acs.jpcb.1c09342
DO - 10.1021/acs.jpcb.1c09342
M3 - Review article
C2 - 35084861
AN - SCOPUS:85124160144
SN - 1520-6106
VL - 126
SP - 1861
EP - 1867
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 9
ER -