C Stefan Voertler

University of Leipzig, Leipzig, Saxony, Germany

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Publications (6)15.29 Total impact

  • Franziska Peter · C. Stefan Voertler
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    ABSTRACT: This chapter contains sections titled: Introduction General Strategy Running the In vitro Selection Cycle Analysis of the Selection Outcome Troubleshooting References
    No preview · Chapter · Mar 2014
  • C.S. Vörtler · M. Milovnikova

    No preview · Article · Feb 2008
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    ABSTRACT: Prokaryotic class I release factors (RFs) respond to mRNA stop codons and terminate protein synthesis. They interact with the ribosomal decoding site and the peptidyl-transferase centre bridging these 75 Å distant ribosomal centres. For this an elongated RF conformation, with partially unfolded core domains II·III·IV is required, which contrasts the known compact RF crystal structures. The crystal structure of Thermus thermophilus RF2 was determined and compared with solution structure of T. thermophilus and Escherichia coli RF2 by microcalorimetry, circular dichroism spectroscopy and small angle X-ray scattering. The structure of T. thermophilus RF2 in solution at 20°C is predominantly compact like the crystal structure. Thermodynamic analysis point to an initial melting of domain I, which is independent from the melting of the core. The core domains II·III·IV melt cooperatively at the respective physiological temperatures for T. thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome.
    Full-text · Article · Feb 2007 · Nucleic Acids Research
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    ABSTRACT: Deactivation of release factor 1 by polyclonal antibodies in an in vitro translation system, which was used to express the esterase gene, led to the reversible elimination of naturally occurring termination. This technique allowed the antibiotic puromycin to be used as an acceptor substrate for the peptidyl residue in the peptidyl-transferase reaction. This resulted in more than 80 % yield of protein with C-terminally incorporated puromycin. pCpPuromycin that was either conjugated with the Cy3 fluorophor or biotin by N4 alkylation of cytosine, also acted as an acceptor substrate for the peptidyl-transferase reaction and was incorporated into the protein C terminus. The resulting conjugates possessed Cy3-specific fluorescence and affinity to streptavidin-coated surfaces, respectively. This left the enzymatic activity of the reporter protein unaffected. It was also shown that extension of puromycin on its 5'-hydroxyl end by up to ten deoxyoligonucleotides also allowed conjugation with the C terminus of in vitro translated protein when RF1-dependent termination was suppressed. However, the conjugation yield decreased upon addition of more than six nucleotides.
    Full-text · Article · Feb 2006 · ChemBioChem
  • M Sprinzl · M Milovnikova · C S Voertler
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    ABSTRACT: Nucleic acid molecules are designed to interact predominantly with proteins or complementary nucleic acids. Interaction of nucleic acids with carbohydrates, abundant constituents of glycoproteins and glycolipids, are not common in cells. Biomedical applications of nucleic acids targeted against oligosaccharides, which are involved in the function of receptors, immune answer, host interaction with invading infectious agents, and cancer metastasis, are feasible. In vitro selection of nucleic acids interacting with oligoand polysaccharides is a promising strategy to identify potential inhibitors of biochemical recognition processes in which carbohydrates are involved. Several RNA and DNA aptamers directed against carbohydrates have already been isolated and characterized. The results are summarized in this article, and an attempt is made to draw initial conclusions concerning the perspectives of the outlined approach.
    No preview · Article · Feb 2006 · Handbook of experimental pharmacology
  • Mathias Sprinzl · C Stefan Voertler
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    ABSTRACT: (Figure Presented) Ribosomal protein biosynthesis is a chemical reaction with remarkable efficiency and fidelity. The chemical mechanisms enabling this remain unclear, despite all the structural insight gained over the years. Recent results on the effect of remote mutations give some clues: the entire tRNA conformation can overrule the codon-anticodon decoding (see figure).
    No preview · Article · Dec 2005 · ChemBioChem