The compact conformation of fibronectin is determined by intramolecular ionic interactions.

@article{Johnson1999TheCC,
  title={The compact conformation of fibronectin is determined by intramolecular ionic interactions.},
  author={Kevin Johnson and Helen Sage and Gina Briscoe and Harold P Erickson},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 22},
  pages={15473-9}
}
Fibronectin exists in a compact or extended conformation, depending upon environmental pH and salt concentration. Using recombinant fragments expressed in bacteria and baculovirus, we determined the domains responsible for producing fibronectin's compact conformation. Our velocity and equilibrium sedimentation data show that FN2-14 (a protein containing FN-III domains 2 through 14) forms dimers in low salt. Experiments with smaller fragments indicates that the compact conformation is produced… CONTINUE READING