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様々な反応サイクル時間をもつGroEL 変異体のデザイン--材料分析室利用研究成果、そのXXIX(3)-- Design of GroEL mutants with various reaction cycle time-- Research works accomplished by using materials analysis facilities:XXIX(3)-- 増田, 恵 Masuda, Megumi 依田, ひろみ Yoda, Hiromi 小池, あゆみ Koike-Takeshita, Ayumi GroEL GroES Chaperonin ATP hydrolysis application/pdf The chaperonin GroEL is an essential multisubunit assemblies that promotes facilitated protein folding in concert with ATP hydrolysis. The Escherichia coli GroEL consists of 14 identical subunits arranged in two heptamer rings. Each ring contains a central cavity and the two rings are stacked back-to-back. GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate to fold, and undergo an ATPregulated interaction cycle to close and open the folding cage. Asp52 and Asp398 in GroEL are known as the critical residues on ATP hydrolysis because GroEL(D52A/D398A) mutant is severely deficient in ATP hydrolysis but not in ATP binding. Here, we investigated the functional role of another amino acid residues facing towards the nucleotide-binding pocket in the crystal structure of GroEL. A series of ATP hydrolysis mutants of GroEL, in which reaction cycle time is 8-sec ~ 6-days, have been constructed for application to DDS carrier. 神奈川工科大学 2019-03-01 jpn departmental bulletin paper VoR https://doi.org/10.34411/00001167 http://hdl.handle.net/10368/32001 https://kait.repo.nii.ac.jp/records/1174 10.34411/00001167 AA12669200 21882878 神奈川工科大学研究報告.B,理工学編 43 21 26 https://kait.repo.nii.ac.jp/record/1174/files/kkb-043-005.pdf application/pdf 1.1 MB 2019-04-04