Protein conformational dynamics dictate the binding affinity for a ligand.

@article{Seo2014ProteinCD,
  title={Protein conformational dynamics dictate the binding affinity for a ligand.},
  author={Moon-Hyeong Seo and Jeongbin Park and Eunkyung Kim and Sungchul Hohng and Hak-Sung Kim},
  journal={Nature communications},
  year={2014},
  volume={5},
  pages={3724}
}
Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand-protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding… CONTINUE READING