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This thesis describes research into the mode of function,
inhibition, and evolution of the ribosomal catalytic center, the
Peptidyl Transferase Center (PTC)--research that has already led to
attempts at improving PTC antibiotics. The PhD candidate carried
out two parallel studies. One using a combination of X-ray
crystallography, biochemistry, molecular biology, and theoretical
studies to obtain crystal structures of ribosomal particles with
antibiotics that target the PTC, revealing the modes of action,
resistance, cross-resistance and discrimination between ribosomes
of eubacterial pathogens and eukaryotic hosts. In the second
parallel study, the candidate synthesized a ribosomal
substructure--one that may represent the minimal entity capable of
catalyzing peptide bond formation--shedding light on the origin of
the ribosome itself.
This thesis describes research into the mode of function,
inhibition, and evolution of the ribosomal catalytic center, the
Peptidyl Transferase Center (PTC)--research that has already led to
attempts at improving PTC antibiotics. The PhD candidate carried
out two parallel studies. One using a combination of X-ray
crystallography, biochemistry, molecular biology, and theoretical
studies to obtain crystal structures of ribosomal particles with
antibiotics that target the PTC, revealing the modes of action,
resistance, cross-resistance and discrimination between ribosomes
of eubacterial pathogens and eukaryotic hosts. In the second
parallel study, the candidate synthesized a ribosomal
substructure--one that may represent the minimal entity capable of
catalyzing peptide bond formation--shedding light on the origin of
the ribosome itself. Content Level Research
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