Conformational changes in a mammalian voltage-dependent potassium channel inactivation peptide.

@article{Abbott1998ConformationalCI,
  title={Conformational changes in a mammalian voltage-dependent potassium channel inactivation peptide.},
  author={Geoffrey W. Abbott and E A Mercer and R Timothy Miller and Bala Ramesh and Surjit Kaila S Srai},
  journal={Biochemistry},
  year={1998},
  volume={37 6},
  pages={1640-5}
}
Fast inactivation is restored in inactivation deletion mutant voltage-gated potassium (Kv) channels by application of synthetic inactivation 'ball' peptide. Using Fourier transform infrared and circular dichroism spectroscopy, we have investigated the structure of synthetic Kv3.4 channel ball peptide, in a range of environments relevant to the function of the ball domain. The ball peptide contains no alpha-helix or beta-sheet in reducing conditions in aqueous solution, but when cosolubilized… CONTINUE READING