Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate.

@article{Hornby2000EquilibriumFO,
  title={Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate.},
  author={Judith A T Hornby and Jack K. Luo and J M Stevens and Louise A Wallace and Warren A. Kaplan and Richard N. Armstrong and Heini W Dirr},
  journal={Biochemistry},
  year={2000},
  volume={39 40},
  pages={12336-44}
}
The conformational stabilities of two homodimeric class mu glutathione transferases (GSTM1-1 and GSTM2-2) were studied by urea- and guanidinium chloride-induced denaturation. Unfolding is reversible and structural changes were followed with far-ultraviolet circular dichroism, tryptophan fluorescence, enzyme activity, chemical cross-linking, and size-exclusion chromatography. Disruption of secondary structure occurs as a monophasic transition and is independent of protein concentration. Changes… CONTINUE READING
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Protein Structure, A Practical Approach

  • C. N. Pace, B. A. Shirley, J. A. Thomson
  • 1989

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