Fluorescence-based monitoring of PAD4 activity via a pro-fluorescence substrate analog.

@article{Sabulski2014FluorescencebasedMO,
  title={Fluorescence-based monitoring of PAD4 activity via a pro-fluorescence substrate analog.},
  author={Mary J Sabulski and Jonathan M. Fura and Marcos M Pires},
  journal={Journal of visualized experiments : JoVE},
  year={2014},
  volume={93},
  pages={e52114}
}
Post-translational modifications may lead to altered protein functional states by increasing the covalent variations on the side chains of many protein substrates. The histone tails represent one of the most heavily modified stretches within all human proteins. Peptidyl-arginine deiminase 4 (PAD4) has been shown to convert arginine residues into the non… CONTINUE READING