Phosphorus-31 nuclear magnetic resonance of ethidium complexes with ribonucleic acid model systems and phenylalanine-accepting transfer ribonucleic acid

Evelyn M. Goldfield, Bruce A. Luxon, Vickie Bowie, David G. Gorenstein

Research output: Contribution to journalArticle

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Abstract

The temperature dependence of the 31P NMR spectra of the ethidium complexes with poly(A)·oligo(U) and the 31P spectra of phenylalanine tRNA (yeast) in various molar ratios of ethidium ion (Et) are presented. In the poly(A)·oligo(U)·Et complex, a new peak about 2.0 ppm downfield from the double-helix peak appears. We have assigned this peak to phosphates perturbed by ethidium. The chemical shift of this peak is consistent with the intercalation mode of binding and provides additional support for our hypothesis that 31P shifts are sensitive probes of phosphate ester conformations. The main effect of ethidium on the 31P spectra of tRNAPhe is the broadening of several of the scattered signals. These scattered signals are associated with phosphates involved in tertiary interactions. We propose that these broadened signals arise from phosphates near the Et binding site.

Original languageEnglish (US)
Pages (from-to)3336-3344
Number of pages9
JournalBiochemistry
Volume22
Issue number14
StatePublished - 1983
Externally publishedYes

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Ethidium
Transfer RNA
Phenylalanine
Phosphorus
Magnetic Resonance Spectroscopy
Poly A-U
Phosphates
Nuclear magnetic resonance
RNA
Poly A
RNA, Transfer, Phe
Chemical shift
Intercalation
Yeast
Conformations
Esters
Yeasts
Binding Sites
Ions
Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorus-31 nuclear magnetic resonance of ethidium complexes with ribonucleic acid model systems and phenylalanine-accepting transfer ribonucleic acid. / Goldfield, Evelyn M.; Luxon, Bruce A.; Bowie, Vickie; Gorenstein, David G.

In: Biochemistry, Vol. 22, No. 14, 1983, p. 3336-3344.

Research output: Contribution to journalArticle

Goldfield, Evelyn M. ; Luxon, Bruce A. ; Bowie, Vickie ; Gorenstein, David G. / Phosphorus-31 nuclear magnetic resonance of ethidium complexes with ribonucleic acid model systems and phenylalanine-accepting transfer ribonucleic acid. In: Biochemistry. 1983 ; Vol. 22, No. 14. pp. 3336-3344.
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AU - Bowie, Vickie

AU - Gorenstein, David G.

PY - 1983

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N2 - The temperature dependence of the 31P NMR spectra of the ethidium complexes with poly(A)·oligo(U) and the 31P spectra of phenylalanine tRNA (yeast) in various molar ratios of ethidium ion (Et) are presented. In the poly(A)·oligo(U)·Et complex, a new peak about 2.0 ppm downfield from the double-helix peak appears. We have assigned this peak to phosphates perturbed by ethidium. The chemical shift of this peak is consistent with the intercalation mode of binding and provides additional support for our hypothesis that 31P shifts are sensitive probes of phosphate ester conformations. The main effect of ethidium on the 31P spectra of tRNAPhe is the broadening of several of the scattered signals. These scattered signals are associated with phosphates involved in tertiary interactions. We propose that these broadened signals arise from phosphates near the Et binding site.

AB - The temperature dependence of the 31P NMR spectra of the ethidium complexes with poly(A)·oligo(U) and the 31P spectra of phenylalanine tRNA (yeast) in various molar ratios of ethidium ion (Et) are presented. In the poly(A)·oligo(U)·Et complex, a new peak about 2.0 ppm downfield from the double-helix peak appears. We have assigned this peak to phosphates perturbed by ethidium. The chemical shift of this peak is consistent with the intercalation mode of binding and provides additional support for our hypothesis that 31P shifts are sensitive probes of phosphate ester conformations. The main effect of ethidium on the 31P spectra of tRNAPhe is the broadening of several of the scattered signals. These scattered signals are associated with phosphates involved in tertiary interactions. We propose that these broadened signals arise from phosphates near the Et binding site.

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