Studies of E. coli Ribosomes Involving Fluorescence Techniques

  • B. Hardesty
  • O. W. Odom
  • W. Rychlik
  • D. Robbins
  • H. Y. Deng
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Most models of the Escherichia coli ribosome and its subunits [see Figs. 2, 4, and 5 in Wittmann (1983)] are based primarily on images obtained by electron microscopy. Information about the spatial arrangements of the individual ribosomal proteins and rRNA2 has come mainly from immune electron microscopy, neutron scattering, and protein-protein cross-linking experiments. Techniques involving fluorescence provide another powerful approach for determining ribosome structure and function. One of the most useful procedures involves determination of distances between pairs of probes by nonradiative singlet-singlet energy transfer. Though the useful range for energy transfer with commonly used donor and acceptor probes is relatively narrow (about 20 Å to 80 Å), this range is compatible with the size of most ribosomal proteins and tRNA. An advantage of this method is that a single fluorophore can be covalently attached to a specific known position, for instance a cysteine in a protein or a terminal nucleotide in an RNA molecule.

Keywords

Ribosomal Protein Rotational Correlation Time Anticodon Loop Extreme Thermophile Immune Electron Microscopy 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer-Verlag, Berlin Heidelberg 1984

Authors and Affiliations

  • B. Hardesty
    • 1
  • O. W. Odom
    • 1
  • W. Rychlik
    • 1
  • D. Robbins
    • 1
  • H. Y. Deng
    • 1
  1. 1.Clayton Foundation Biochemical Institute, Department of ChemistryUniversity of TexasAustinUSA

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