Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded alpha-helical coiled-coils.

@article{Kohn1997PositionalDO,
  title={Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded alpha-helical coiled-coils.},
  author={Wayne D Kohn and Cyril M. Kay and Robert S. Hodges},
  journal={Journal of peptide science : an official publication of the European Peptide Society},
  year={1997},
  volume={3 3},
  pages={
          209-23
        }
}
The effects on protein stability of negatively charged Glu side chains at different positions along the length of the alpha-helix were investigated in the two-stranded alpha-helical coiled-coil. A native coiled-coil has been designed which consists of two identical 35 residue polypeptide chains with a heptad repeat QgVaGbAcLdQeKf and a Cys residue at position 2 to allow the formation of an interchain 2-2' disulphide bridge. This coiled-coil contains no intra- or interchain electrostatic… CONTINUE READING