Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system.

@article{Chu1998ThermodynamicAS,
  title={Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system.},
  author={Vano Chu and S. Freitag and Isolde Le Trong and Ronald E. Stenkamp and Patrick S. Stayton},
  journal={Protein science : a publication of the Protein Society},
  year={1998},
  volume={7 4},
  pages={848-59}
}
A circularly permuted streptavidin (CP51/46) has been designed to remove the flexible polypeptide loop that undergoes an open to closed conformational change when biotin is bound. The original termini have been joined by a tetrapeptide linker, and four loop residues have been removed, resulting in the creation of new N- and C-termini. Isothermal titration… CONTINUE READING