Abstract
Rotational relaxation on the microsecond time scale has been followed by a depolarization technique using the properties of the long-lived triplet state of covalently bound labels. Two triplet probes, which efficiently bind to ribosomal proteins, are described. The rotational correlation time of 70S ribosomes of Escherichia coli has been measured. The average hydrodynamic radius of the functionally active 70S particle in solution has been estimated to 147 A. A concentration dependence of the correlation time has been observed, which may result from an association of the 70S ribosomes to form 100S dimers.
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