Dynamical properties of the loop 320s of substrate-free and substrate-bound muscle creatine kinase by NMR: evidence for independent subunits.

@article{Rivire2012DynamicalPO,
  title={Dynamical properties of the loop 320s of substrate-free and substrate-bound muscle creatine kinase by NMR: evidence for independent subunits.},
  author={Gwladys Rivi{\`e}re and Maggy Hologne and Olivier Marcillat and Jean-Marc Lancelin},
  journal={The FEBS journal},
  year={2012},
  volume={279 16},
  pages={2863-75}
}
Muscle creatine kinase (MCK; EC2.7.3.2) is a 86 kDa homodimer that belongs to the family of guanidino kinases. MCK has been intensively studied for several decades, but it is still not known why it is a dimer because this quaternary structure does not translate into obvious structural or functional advantages over the homologous monomeric arginine kinase… CONTINUE READING