Tokyo Institute of Technology · 생화학·유전·분자생물학
히데키 타구치 교수의 연구실은 단백질 접힘과 응고, 특히 채플론린과 같은 분자량 보조 단백질이 단백질의 올바른 접힘에 어떻게 기여하는지에 중점을 두고 있습니다. 또한 유전자 발현의 비가역적 변화를 유도하는 페리온 단백질의 구조적 특성과 동적 거동을 고속 원자력 현미경, 전자현미경, 단일세포 분석 기법을 통해 실시간으로 관찰하고 있습니다. 이는 단백질 축적과 관련된 질병 메커니즘을 밝히는 데 기여합니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
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
