Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.

@article{Werner1989AnalysisOT,
  title={Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.},
  author={William E Werner and Howard K Schachman},
  journal={Journal of molecular biology},
  year={1989},
  volume={206 1},
  pages={221-30}
}
A global conformational change in the regulatory enzyme aspartate transcarbamoylase of Escherichia coli was demonstrated 20 years ago by the 3.5% decrease in the sedimentation coefficient of the enzyme upon its interaction with carbamoyl phosphate and saturating amounts of the aspartate analog succinate. This "swelling" of aspartate transcarbamoylase attributable to the T----R allosteric transition was observed also in subsequent studies when the enzyme was completely saturated with the… CONTINUE READING