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Updated: Jul 25, 2026

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
Published on: February 4, 2013
A part of ice nucleation protein exhibits the ice-binding ability
Yoshihiro Kobashigawa1, Yoshiyuki Nishimiya, Kazunori Miura
1Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), Toyohira, Sapporo 062-8517, Japan.
Abstract:
We generated a recombinant 96-residue polypeptide corresponding to a sequence Tyr176-Gly273 of ice nucleation protein from Pseudomonas syringae (denoted INP96). INP96 exhibited an ability to shape an ice crystal, whose morphology is highly similar to the hexagonal-bipyramid generally identified for antifreeze protein. INP96 also showed a non-linear, concentration-dependent retardation of ice growth. Additionally, circular dichroism and NMR measurements suggested a local structural construction in INP96, which undergoes irreversible thermal denaturation. These data imply that a part of INP constructs a unique structure so as to interact with the ice crystal surfaces.
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