Analysis of the Molecular Recognition of L-Isoleucine, by Isoleucyl-tRNA Synthetase
1987 Volume 1987 Issue 3 Pages 402-404
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1987 Volume 1987 Issue 3 Pages 402-404
The 400-MHz 1H-NMR spectra of L-isoleucine were measured in the presence of Escherichia coli isoleucyl-tRNA synthetase (IleRS). Because of chemical exchange of L-isoleucine between the free state ang the IleRS-bound state, transferred nuclear Overhauser effect (TRNOE) was observed among proton resonances of L-isoleucine. The IleRS-bound L-isoleucine was found to take the gauche+ form about the Cα-Cβ bond and the trans form about the Cβ-Cγ1 bond. The TRNOE analysis is useful for studying the amino acid discrimination mechanism of aminoacyl-tRNA synthetases.
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