Protein Synthesis and Ribosome Structure

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Knud H. Nierhaus, Daniel Wilson
Wiley, Oct 15, 2004 - Science - 579 pages
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Knud Nierhaus, who has studied the ribosome for more than 30 years, has assembled here the combined efforts of several scientific disciplines into a uniform picture of the largest enzyme complex found in living cells, finally resolving many decades–old questions in molecular biology. In so doing he considers virtually all aspects of ribosome structure and function –– from the molecular mechanism of different ribosomal ribozyme activities to their selective inhibition by antibiotics, from assembly of the core particle to the regulation of ribosome component synthesis. The result is a premier resource for anyone with an interest in ribosomal protein synthesis, whether in the context of molecular biology, biotechnology, pharmacology or molecular medicine.

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About the author (2004)

Knud H. Nierhaus studied medicine and completed his thesis with Prof. Klaus Betke in Tübingen (Germany). In 1968 he joined the Max–Planck–Institut für Molekulare Genetik in Berlin, where he currently leads a research group studying different aspects of translation. He is "außerplanmäßiger Professor" at the TU, Berlin and "adjunct Professor" at the Moscow State University. His main achievements include the development of a method to reconstitute the large subunit from E. coli ribosomes from its isolated components and the detection of a third tRNA binding site, the E site, on the ribosome. Daniel N. Wilson studied Biochemistry and Molecular Biology at Victoria University, Wellington (New Zealand). He carried out his PhD in the laboratory of Prof. Warren Tate in the Biochemistry Department at the University of Otago, Dunedin. In his thesis he focused on the mechanisms of translational termination and recoding events. Following completion of his studies in 1999, he was awarded an Alexander von Humboldt fellowship and currently works on the crystallography of ribosomes at the Max–Planck–Institut für Molekulare Genetik in Berlin.

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