The conformation of nascent polylysine and polyphenylalanine peptides on ribosomes

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Issue Date
1991-01-25Author
Picking, William D.
Odom, Obed W.
Tsalkova, Tamara
Serdyuk, Igor
Hardesty, Boyd
Publisher
American Society for Biochemistry and Molecular Biology
Type
Article
Article Version
Scholarly/refereed, publisher version
Published Version
www.jbc.org/content/266/3/1534.abstractRights
This research was originally published in Journal of Biological Chemistry. W. D. Picking, O. W. Odom, T. Tsalkova, I. Serdyuk and B. Hardesty . The conformation of nascent polylysine and polyphenylalanine peptides on ribosomes. Journal of Biological Chemistry. 1991; 266, 1534-1542. © the American Society for Biochemistry and Molecular Biology.
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Show full item recordAbstract
Polypeptide synthesis using either phenylalanine or lysine was initiated on Escherichia coli ribosomes; then the position and conformation of the nascent peptide were monitored by fluorescence techniques. To this end, fluorophores had been attached to the amino terminus of each nascent peptide, and major differences were observed as chain extension occurred. Polyphenylalanine appeared to build up as a hydrophobic mass adjacent to the peptidyl transferase center while polylysine apparently was extended directly from the ribosome into the surrounding solution. An explanation for these differences may be provided by the physical and chemical properties of each polypeptide. These properties may be responsible for the route by which each peptide exits the peptidyl transferase center as demonstrated by the different sensitivity of each to inhibition by erythromycin.
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Citation
Picking, W. D., Odom, O. W., Tsalkova, T., Serdyuk, I., & Hardesty, B. (1991). The conformation of nascent polylysine and polyphenylalanine peptides on ribosomes. Journal of Biological Chemistry, 266(3), 1534-1542.
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