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Identifier uch.biology.msc//2006plati
Title Καθαρισμός και Διερεύνηση Κρυσταλλογένεσης του Μεταλλάγματος Cys 23 Ala της Pseudomonas syringae pv phaseolicola
Creator Plati, Ioanna
Abstract The type III secretion system is a transporter mechanism of gram-negative bacterial effectors. HrcQb of the Psudomonas syringae is a conserved component of the type III secretion apparatus in gram-negative bacteria. The C-terminal region of this protein, the 79 residues, is the part where significant similarities with the homologous proteins are observed. These homologous proteins also participate in the export mechanism for the flagellum assembly. The crystal structure, as determined by Dr. V. Fadouloglou, of HrcQb-C is an elongated, gently curved homotetramer which can be characterized as an overwhelmingly beta-structure. We focused on the mutation C23A of HrcQb-C, and on the impact in crystallization of the absence of the disulfide bond. The molecule C23A HrcQb-C was overexpressed in E.coli cells and purified. Unfortunatelly, all the crystallization attempts were unsuccessfull as the molecule was very sensitive to proteolysis even in the presence of protein inhibitors at low temperatures.
Issue date 2006-09-01
Date available 2006-11-13
Collection   School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Post-graduate theses
Permanent Link https://elocus.lib.uoc.gr//dlib/f/c/f/metadata-dlib-2006plati.tkl Bookmark and Share
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