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Hot on the heels of his Nobel Prize in Chemistry, Venkatraman Ramakrishnan and his colleague T. Martin Schmeing summarise what studies of the structure and function of the ribosome have revealed and their hopes for the future. They conclude: "one can only look back in wonder at the rate of progress in the last decade in our understanding of many key aspects of the translation pathway."
The ribosome is the large ribonucleoprotein particle that assembles proteins in all cells. In their Review, published online in Nature, the authors focus on the intricate network of reactions that underlie bacterial translation, which are common to the synthesis of all proteins. They argue that although a complete understanding of translation has yet to be achieved; knowledge of the ribosome structure drives increasingly sophisticated biochemical and genetic experimentation. Furthermore, the use of molecular dynamics and biophysical techniques are now allowing scientists to comprehend not just what steps are involved, but how the ribosome proceeds from one state to the next. In addition to their impact on basic translation research, the structures have also provided a framework for the development of better antibiotics. CONTACT Venkatraman Ramakrishnan (MRC Laboratory of Molecular Biology, Cambridge, UK)
E-mail: ramak@mrc-lmb.cam.ac.uk Martin Schmeing (MRC Laboratory of Molecular Biology, Cambridge, UK)
E-mail: schmeing@mrc-lmb.cam.ac.uk (C) Nature press release.
Message posted by: Trevor M. D'Souza
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