| Description |
1 online resource (xiii, 74 pages) : illustrations (some color) |
| Series |
Springer theses |
|
Springer theses.
|
| Contents |
Introduction -- Methods -- Results -- Discussion |
| Summary |
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 |
| Analysis |
nucleic acids |
|
ribosomen |
|
ribosomes |
|
eiwitten |
|
proteins |
|
Cellular Biology |
|
Celbiologie |
| Notes |
Ph. D. Weizmann Institute of Science |
| Bibliography |
Includes bibliographical references |
| Notes |
Print version record |
| Subject |
Ribosomes.
|
|
RNA polymerases.
|
|
Antibiotics -- Biotechnology
|
|
Ribosomes
|
|
DNA-Directed RNA Polymerases
|
|
SCIENCE -- Life Sciences -- Biochemistry.
|
|
Antibiotics -- Biotechnology
|
|
Ribosomes
|
|
RNA polymerases
|
| Genre/Form |
dissertations.
|
|
Academic theses
|
|
Academic theses.
|
|
Thèses et écrits académiques.
|
| Form |
Electronic book
|
| ISBN |
9783642169311 |
|
3642169317 |
|
