Kobashigawa Yoshihiro, Nishimiya Yoshiyuki, Miura Kazunori, Ohgiya Satoru, Miura Ai, Tsuda Sakae
Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), Toyohira, Sapporo 062-8517, Japan.
FEBS Lett. 2005 Feb 28;579(6):1493-7. doi: 10.1016/j.febslet.2005.01.056.
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.
我们生成了一种重组96个氨基酸的多肽，其对应于丁香假单胞菌冰核蛋白序列Tyr176 - Gly273（表示为INP96）。INP96表现出塑造冰晶的能力，其形态与通常鉴定的抗冻蛋白的六方双锥体高度相似。INP96还表现出冰生长的非线性、浓度依赖性延迟。此外，圆二色性和核磁共振测量表明INP96中存在局部结构构建，其经历不可逆的热变性。这些数据表明，INP的一部分构建了独特的结构以便与冰晶表面相互作用。
