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. 2022 Jan 27;126(9):1861–1867. doi: 10.1021/acs.jpcb.1c09342

Figure 1.

Figure 1

Overview of the proposed structure and working mechanism of bacterial ice nucleation proteins anchored to the outer cell membrane of P. syringae. The INP consists of an N-terminal, a C-terminal, and a central repeating domain. Their general function is to order water molecules into an “ice-like” arrangement to nucleate ice formation. This process is facilitated when INPs assemble into larger aggregates.