Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein.

@article{Shao1997ConstructionAC,
  title={Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein.},
  author={X. Shao and Preston Hensley and Charles R. Matthews},
  journal={Biochemistry},
  year={1997},
  volume={36 32},
  pages={9941-9}
}
Tryptophan repressor (TR) from Escherichia coli is a homodimer whose highly helical subunits intertwine in a complex fashion. A monomeric version of Trp repressor has been constructed by introducing a pair of polar amino acids at the hydrophobic dimer interface. Analytical ultracentrifugation was used to show that the replacement of leucine at position 39… CONTINUE READING