Abstract
YEAST tRNA3Leu is one of the more thoroughly investigated tRNA species because it can exist in two conformations which can be interconverted1–5. The native (N) conformer has full biochemical activity, whereas the denatured (D) conformer is inactive with respect to aminoacylation. Although other tRNAs can be reversibly denatured6–8, the D conformer of yeast tRNA3Leu is quite stable1–5. Because of these properties, yeast tRNA3Leu has been studied in the hope that it might provide insight into the synthetase recognition problem. This aim has been thwarted, however, by lack of information on the secondary structure of the D conformer. Even less is known about the tertiary structure of this molecule in solution.
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KEARNS, D., WONG, Y., HAWKINS, E. et al. Biological Sciences: Model for the Secondary Structure of the Denatured Conformer of Yeast tRNA3Leu. Nature 247, 541–543 (1974). https://doi.org/10.1038/247541a0
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DOI: https://doi.org/10.1038/247541a0
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