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한성구,진봉석,이원규,유연규 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.8
In this study, the kinetic properties of wild-type and C117D mutant H. influenzae MurA (Hi MurA), which catalyzes the first reaction in the biosynthetic pathway of the cell wall, were characterized. Purified recombinant Hi MurA was active at pH values ranging from pH 5.5 to pH 10, and its Km (UNAG), Km (PEP),and k_(cat) values were measured to be 31 μM, 24 μM, and 210 min^−1, respectively. Hi MurA activity was effectively inhibited by fosfomycin with an IC_50 value of 60 μM. Hi MurA contains a cysteine residue (C117)at the loop region near the PEP binding, whereas MurA from fosfomycin resistant Mycobaterium tuberculosis or Chlamydia trachomatis contain an aspartate residue instead of the cysteine at the corresponding site. Aspartate substitution of Cys117 in Hi MurA shifted its optimum pH from 7.8 to 6.0. In addition, the K_m values for UNAG and PEP were increased to 160 μM and 150 μM, respectively, and the k_(cat) value was significantly reduced to 41 min^−1. Furthermore, the C117D mutant form of Hi MurA was not inhibited by 1 mM fosfomycin. These results indicate that the Cys117 of Hi MurA is the binding site of fosfomycin and plays an important role in the fast turnover of the catalytic reaction.
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A Cell-based Method to Monitor the Interaction between Hepatitis B Virus Capsid and Surface Proteins
Yun-Kyoung Kim,Soo-Jin Oh,진봉석,Chanhoo Park,Hyesung Jeon,Doo Wan Boo,Yeon Gyu Yu 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.3
Interactions between the surface and capsid proteins of the hepatitis B virus (HBV) are critical for the assembly of virus particles. In this study, we developed a cell-based method to visualize the interactions between the capsid and surface proteins of HBV. Capsid-GFP, a capsid protein fused to a green fluorescence protein (GFP), forms nucleocapsid-like structures in the cytoplasm of mammalian cells. It relocates to the plasma membranes in cells expressing PH-PreS, a fusion protein consisting of the PreS region of the HBV surface protein and the PH domain of PLC-γ. Membrane localization of the capsid-GFP in these cells is prevented by an inhibitory peptide that blocks the interaction between the capsid and surface proteins. This dynamic localization of capsid-GFP is applicable for screening compounds that may potentially inhibit or prevent the assembly process of HBV particles.
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