Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872728 | FEBS Letters | 2005 | 5 Pages |
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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Authors
Yoshihiro Kobashigawa, Yoshiyuki Nishimiya, Kazunori Miura, Satoru Ohgiya, Ai Miura, Sakae Tsuda,