25 research outputs found
Ein Experimenteller Nachweis der Resorption von Desoxycorticosteron und Desoxycorticosteronacetat bei Percutaner und Peroraler Darreichung
�ber die Implantation von Testosteron-Presslingen in den menschlichen Hoden und die dadurch erreichte Entwicklung des Keimepithels
Über die Luteinisierende Wirkung des Follikelhormons Durch Beeinflussung der Luteogenen Hypophysenvorder-Lappensekretion
Structural and Thermodynamic Characterization of Vibrio fischeri CcdB*
CcdBVfi from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdBVfi is a dimer that unfolds to the corresponding monomeric components in a two-state fashion. In the unfolded state, the monomer retains a partial secondary structure. This observation correlates well with the crystal and NMR structures of the protein, which show a dimer with a hydrophobic core crossing the dimer interface. In contrast to its F plasmid homologue, CcdBVfi possesses a rigid dimer interface, and the apparent relative rotations of the two subunits are due to structural plasticity of the monomer. CcdBVfi shows a number of non-conservative substitutions compared with the F plasmid protein in both the CcdA and the gyrase binding sites. Although variation in the CcdA interaction site likely determines toxin-antitoxin specificity, substitutions in the gyrase-interacting region may have more profound functional implications