Hierarchical assembly and environmental enhancement of bacterial ice nucleators.

ABSTRACT: Bacterial ice nucleating proteins (INPs) are exceptionally effective in promoting the kinetically hindered transition of water to ice. Their efficiency relies on the assembly of INPs into large functional aggregates, with the size of ice nucleation sites determining activity. Experimental freezing spectra have revealed two distinct, defined aggregate sizes, typically classified as class A and C ice nucleators (INs). Despite the importance of INPs and years of extensive research, the precise number of INPs forming the two aggregate classes, and their assembly mechanism have remained enigmatic. Here, we report that bacterial ice nucleation activity emerges from more than two prevailing aggregate species and identify the specific number of INPs responsible for distinct crystallization tempera

SUBMITTER: Renzer G 

PROVIDER: S-EPMC11513900 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature