Subtle dynamics of holo glutamine binding protein revealed with a rigid paramagnetic probe.

@article{Liu2014SubtleDO,
  title={Subtle dynamics of holo glutamine binding protein revealed with a rigid paramagnetic probe.},
  author={Zhu Liu and Z. X. Gong and Da-Chuan Guo and W. P. Zhang and Chun Tang},
  journal={Biochemistry},
  year={2014},
  volume={53 9},
  pages={1403-9}
}
Bacterial periplasmic binding proteins (PBPs) are involved in the translocation of small molecules in the periplasm. To unload, the two domains of a PBP open up, allowing the ligand to exit. However, it is not clear whether there are dynamics near the binding site which can facilitate the rapid dissociation of a ligand. To visualize such dynamics, we utilized paramagnetic relaxation enhancement (PRE) NMR and introduced a rigid paramagnetic probe to a PBP, glutamine-binding protein (QBP) with… CONTINUE READING