Anticodon conformation and accessibility in wild-type and suppressor tryptophan tRNA from E. coli.

Abstract

The association between Trp-tRNA and Pro-tRNA, which have complementary anticodon sequences, has been used as a probe of anticodon conformation. It is unaffected, however, by the base change in the D-stem present in UGA-suppressor Trp-tRNA. This does not support the hypothesis that UGA suppression depends upon a conformational change induced in the anticodon. The stable denatured form of wild-type Trp-tRNA no longer interacts with Pro-tRNA; the structure of the anticodon region must therefore be quite different in the denatured form.

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Cite this paper

@article{Buckingham1976AnticodonCA, title={Anticodon conformation and accessibility in wild-type and suppressor tryptophan tRNA from E. coli.}, author={R. H. Buckingham}, journal={Nucleic acids research}, year={1976}, volume={3 4}, pages={965-75} }