Water, logged.

  • Published 2013 in Biopolymers


The kinetic principles underlying an enzyme’s interaction with its substrate offer critical insights into that enzyme’s biological function, and can inform the development of clinically useful molecules that enhance or prevent ligand binding. For hydrophobic target-ligand associations, the purging of water molecules from the binding pocket is a critical step. However, the detailed behavior of solute and solvent during this ‘drying transition’ is incompletely understood. Mondal et al. have built on previous research to perform a detailed molecular dynamics simulation of how this drying transition occurs during the hydrophobic association between a simplified spherical ligand and concave enzyme binding site.

DOI: 10.1002/bip.22373

Cite this paper

@article{2013WaterL, title={Water, logged.}, author={}, journal={Biopolymers}, year={2013}, volume={99 11}, pages={v-vi} }