Tokyo Institute of Technology · Biochemistry, Genetics and Molecular Biology
Professor Hideki Taguchi's research lab specializes in the structural and functional analysis of protein folding chaperones, prion biology, and the self-assembly of amyloidogenic proteins. The lab employs advanced biophysical techniques such as cryo-electron microscopy, high-speed atomic force microscopy, and fluorescence correlation spectroscopy to investigate the dynamics of protein aggregates in living cells and in vitro. A central focus is understanding how intrinsically disordered proteins like Sup35 form pathological or functional amyloid fibrils, and how molecular chaperones such as GroEL-GroES and thermophilic chaperonins facilitate proper protein folding under extreme conditions. The lab also explores the synthesis and characterization of functional oxide materials, particularly perovskite-type manganites, via low-temperature sol-gel processes for potential applications in energy and catalysis.
Figures are computed from collected data and may differ slightly.
Perovskite‐type (La 1‐ x Sr x )MnO 3 (0 x 0.3) was synthesized through the sol–gel process at low temperature (400° to 500°C). Poly(acrylic acid) (PAA) was used to make a gel from an aqueous solution of lanthanum, strontium, and manganese nitrates. The particle‐diameter distribution of the manganites had a maximum value of 0.3 to 0.7 μ m, and a specific surface area of about 17.5 to 23.5 m 2 /g.
A chaperonin has been purified from a thermophilic bacterium, Thermus thermophilus. It consists of two kinds of proteins with approximate Mr 58,000 and 10,000 and shows a 7-fold rotational symmetry from the top view and a "football"-like shape from the side view under the electron microscopic view. Its weak ATPase activity is inhibited by sulfite and activated by bicarbonate. ATP causes change of its mobility in nondenaturating polyacrylamide gel electrophoresis. The T. thermophilus chaperonin c
Yeast prion [PSI+] is caused by aggregated structures of the Sup35 protein. Although Sup35 forms typical amyloid fibrils in vitro, there is no direct evidence for the fibrillar structures of Sup35 in vivo. We analyzed [PSI+] cells in which Sup35 fused with green fluorescent protein (GFP) formed aggregates visible by fluorescence microscopy using thin-section electron microscopy (EM). Rapid-freeze EM combined with an immunogold-labeling technique as well as correlative light EM, which allows high
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