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Targeting Functional Centers of the Ribosome [electronic resource] / by Chen Davidovich.

By: Davidovich, Chen [author.].
Contributor(s): SpringerLink (Online service).
Material type: materialTypeLabelBookSeries: Springer Theses: Publisher: Berlin, Heidelberg : Springer Berlin Heidelberg, 2011Description: XIV, 74 p. online resource.Content type: text Media type: computer Carrier type: online resourceISBN: 9783642169311.Subject(s): Life sciences | Chemistry, Organic | Nucleic acids | Biochemistry | Life Sciences | Nucleic Acid Chemistry | Protein Science | Organic ChemistryDDC classification: 572.84 Online resources: Click here to access online
Contents:
Introduction -- Methods -- Results -- Discussion.
In: Springer eBooksSummary: 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.
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Introduction -- Methods -- Results -- Discussion.

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.

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