作者: R Andrew Marshall
DOI:
关键词:
摘要: The ribosome, a two-subunit macromolecular enzyme comprised of RNA and protein components, interprets genetic code stored on messenger RNA and catalyzes peptide bond formation during the highly regulated translation phase of gene expression. Decades of biochemical and structural studies have revealed that both, local and global structural rearrangements of the ribosome are central to its function, yet our understanding of how ribosome conformational dynamics control translation has been limited by the complexity of the ribosome, itself, and the repetitive, multi-step nature of the process. In this thesis, I report a collection of studies aimed at understanding how changes in ribosome architecture participate in the mechanisms by which protein synthesis regulated. First, using nuclear magnetic resonance (NMR) techniques, the solution structure of a unique aminoglycoside, apramycin, was solved in complex …