Abstract
We have observed well-resolved 31P resonances at 65 kG (109 MHz) in solutions of Escherichia coli tRNAGlu and yeast tRNAPhe. One resolved resonance, identified as the terminal phosphate, titrates with a pK = 6.35. Upon melting the yeast tRNAPhe in 0.1 M NaCl, without Mg++, the resolved peaks broaden and disappear in the vicinity of 35 degrees while the central cluster narrows drastically, shifts slightly, and loses its structure. Addition of Mg++ shifts one resolved peak and changes the shape of the cluster. The 31P lines are broader when observed at 65 kG than at 24 kG. The broadening is shown to come from chemical shift anisotropy which is estimated to be about 140 ppm.
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