Summary
Exchange lifetimes of amide protons intrp-repressor with and without the corepressor,l-tryptophan, were studied by heteronuclear 2D NMR spectroscopy. The amide proton exchange times revealed pronounced differences in the stability of different regions of thetrp-repressor. The dimeric core of the molecule is relatively compact and homogeneous in terms of the measured parameters in both apo- and holorepressors. On the other hand the DNA-binding region appears less stable and more susceptible to the exchange of its backbone protons with the solvent. The NMR findings reported here are consistent with and amplify information on the stability of thetrp-repressor obtained by other methods.
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Dedicated to the memory of Professor V.F. Bystrov
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Czaplicki, J., Arrowsmith, C. & Jardetzky, O. Segmental differences in the stability of thetrp-repressor peptide backbone. J Biomol NMR 1, 349–361 (1991). https://doi.org/10.1007/BF02192859
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DOI: https://doi.org/10.1007/BF02192859