## Abstract The thermal unfolding of yeast phenylalanine‐specific tRNA (tRNA^Phe^) has been calorimetrically investigated at several salt concentrations in the absence of magnesium. Application of the deconvolution theory of macromolecular conformational transitions allows calculation of the thermo
Energy transfer in tRNAPhe (Yeast). The solution structure of transfer RNA
✍ Scribed by W. E. Blumberg; R. E. Dale; J. Eisinger; D. M. Zuckerman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 767 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
In the preceding paper, the dependence of the dipolar orientation factor κ^2^, which governs long‐range (Förster) energy transfer, on the relative orientation and reorientational freedom of the donor and acceptor chromophores is examined. The analysis given there is employed to derive minimum and maximum values of 〈κ^2^〉 for energy transfer from the Y base of tRNA^Phe^ (yeast) to an acriflavine acceptor attached to the 3′ terminus of the tRNA using estimates for the reorientational freedom of the donor derived from a combination of steady‐state and time‐dependent polarized emission measurements. The acceptor motion is estimated from data in the literature. From these limiting values of 〈κ^2^〉 and Beardsley and Cantor's determination of the long range energy‐transfer efficiency for this donor–acceptor pair, the interchromophore distance R is calculated to be between 34 and 61 Å, this range being independent of the particular model chosen to described the reorientational freedom of the donor and acceptor. While this large range in R is of little help in establishing the solution structure of tRNA, the analysis illustrates the potential of polarized energy‐transfer experiments, particularly when transfer depolarization experiments are possible.
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