Ribosomal Proteins of E. coli: Stoichiometry and Implications for Ribosome Structure
This extract was created in the absence of an abstract.
Excerpt
As a step in the investigation of the structure and function of ribosomes several laboratories initiated chemical studies on the ribosomal protein of E. coli (Waller, 1964; Traut, 1966; Traut, Moore, Delius, Noller, and Tissières, 1967; Kaltschmidt, Dzionara, Donner, and Wittmann, 1967; Möller and Chrambach, 1967; Fogel and Sypherd, 1968; Otaka, Itoh, and Osawa, 1968; Craven, Voynow, Hardy, and Kurland, 1969). The major result of these studies was the demonstration that there were a large number of proteins which could be separated by standard techniques. Other laboratories undertook investigations emphasizing functional properties of ribosomal proteins and elegantly showed their functional heterogeneity (Hosokawa, Fujimura, and Nomura, 1966; Staehelin and Meselson, 1966; Nomura, Mizushima, Ozaki, Traub, and Lowry, this volume; Staehelin, Maglott, and Monro, this volume).
In this laboratory the aim has been to answer the following questions: “How many proteins are there?” “To what extent are they different from each other?”...
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↵* Present address: Cold Spring Harbor Laboratory of Quantitative Biology, Cold Spring Harbor, N.Y.
