Andere Kunden interessierten sich auch für
![Dioxygen Binding and Sensing Proteins]( "Dioxygen Binding and Sensing Proteins")
Dioxygen Binding and Sensing Proteins125,99 €![Protein Synthesis and Ribosome Structure]( "Protein Synthesis and Ribosome Structure")
Protein Synthesis and Ribosome Structure172,99 €![Carbohydrate-Based Interactions at the Molecular and the Cellular Level]( "Carbohydrate-Based Interactions at the Molecular and the Cellular Level")
Carbohydrate-Based Interactions at the Molecular and the Cellular Level74,99 €![Biotransformations]( "Biotransformations")
Biotransformations42,99 €![Immobilisation of DNA on Chips II]( "Immobilisation of DNA on Chips II")
Immobilisation of DNA on Chips II249,99 €![Complex Flavoproteins, Dehydrogenases and Physical Methods]( "Complex Flavoproteins, Dehydrogenases and Physical Methods")
Complex Flavoproteins, Dehydrogenases and Physical Methods162,99 €![Membrane Proteins in Aqueous Solutions]( "Membrane Proteins in Aqueous Solutions")
Membrane Proteins in Aqueous Solutions148,99 €
Targeting Functional Centers of the Ribosome investigates the mode of function, inhibition, and evolution of the Peptidyl Transferase Center (PTC) by a combination of X-ray crystallography, biochemistry, molecular biology and theoretical studies.
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.