Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor.

@article{Gloss1997UreaAT,
  title={Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor.},
  author={L. Gloss and Charles R. Matthews},
  journal={Biochemistry},
  year={1997},
  volume={36 19},
  pages={5612-23}
}
The urea-induced equilibrium unfolding of the Escherichia coli Trp repressor (TR) is a two-state process, involving the native dimeric and unfolded monomeric species. Kinetic studies, however, reveal the presence of transient intermediates that appear only during the folding of the 107-residue protein [Gittelman, M. G., & Matthews, C. R. (1990) Biochemistry 29, 7011-7020]. In order to gain insight into the complex kinetic folding mechanism, the sequence of TR was reduced to the amino-terminal… CONTINUE READING

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