Structure-based characterization and antifreeze properties of a hyperactive ice-binding protein from the Antarctic bacterium Flavobacterium frigoris PS1.

@article{Do2014StructurebasedCA,
  title={Structure-based characterization and antifreeze properties of a hyperactive ice-binding protein from the Antarctic bacterium Flavobacterium frigoris PS1.},
  author={Hackwon Do and Soon-jong Kim and Hak Jun Kim and Jun Hyuck Lee},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2014},
  volume={70 Pt 4},
  pages={1061-73}
}
Ice-binding proteins (IBPs) inhibit ice growth through direct interaction with ice crystals to permit the survival of polar organisms in extremely cold environments. FfIBP is an ice-binding protein encoded by the Antarctic bacterium Flavobacterium frigoris PS1. The X-ray crystal structure of FfIBP was determined to 2.1 Å resolution to gain insight into its ice-binding mechanism. The refined structure of FfIBP shows an intramolecular disulfide bond, and analytical ultracentrifugation and… CONTINUE READING

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