| Co-Investigator(Kenkyū-buntansha) |
YURA Kei Nagoya Univ., Grad. Schi. Sci., Res. Assoc, 大学院・理学研究科, 助手 (50252226)
NISHIKAWA Ken Center for Info. Biol., Professor, 生命情報研究センター, 教授 (10093288)
WAKO Hiroshi Schl. Soc. Sci., Waseda Univ., Professor, 社会科学部, 教授 (60158607)
YOMO Tetsuya Grad. Schi. Eng., Osaka Univ., Res. Assoc., 大学院・工学研究科, 助手 (00222399)
ISHIMORI Koichiro Grad. Schi. Eng., Kyoto Univ., Assoc. Prof., 大学院・工学研究科, 助教授 (20192487)
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| Research Abstract |
Natural history group (Go, Yura, Wako, Nishikawa, Mitaku, and Umeyama)
From a classification of the spatial arrangements of the secondary structure elements, Go discovered 'the symmetry rule', whish states that apair of similar protein folds, having no common ancestor, tend to possessan internal symmetry in their fold. Yura found two types of 'modules', a phosphate binding module observed commonly in polymerases and transcription factors, and a substrate-specificity determining module of peroxidases. A newly developed method for detecting similarity in the atomic level revealed a lot of similar ATP binding structures in totally different folds (Go). Wako developed an efficient algorithm of expressing the local environment by a code representation. A new secondary structure prediction method was developed by Nishikawa, who applied the threading method for this purpose. As for the structural prediction for membrane bound proteins, Mitaku improved his method to predict the structure of bacteriorhodopsin correctly. Umeyama established a fully automated algorithm of homology modeling, which is estimated to give a sufficient accuracy.
Design group (Yomo and Ishimori)
Yomo found in random mutagenesis experiments on catalase that the thermal stability and activity of the protein is extremely robust against mutations, and that a possibility of the functional optimization by the evolutional engineering technique can enormously enhanced by the elongation of the chain length. The concept of 'module' was applied to produce chimera hemoglobin, which was synthesized by exchanging its modules each other. From such chimera proteins, Ishimori confirmed that the structural unit, module, works not only as the unit of maintaining the protein stability, but also as a unit for realizing the function of hemoglobin.
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