Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions.

@article{GordonSmith2001SolutionSO,
  title={Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions.},
  author={Debbie-Ann Gordon-Smith and Rodrigo J. Carbajo and Katherine Stott and David Neuhaus},
  journal={Biochemical and biophysical research communications},
  year={2001},
  volume={280 3},
  pages={855-60}
}
Mutants of chymotrypsin inhibitor protein 2 have previously been studied in which 4 or 10 glutamine residues were inserted into the inhibitory loop of the protein between residues 59 and 60, as potential models for the behaviour of glutamine tracts in proteins associated with polyglutamine-expansion neurodegenarative diseases. These mutants form very stable monomers, dimers and trimers. Although the cause of oligomerisation was found to be domain-swapping, it was thought that the glutamine… CONTINUE READING