Weakly hydrated surfaces and the binding interactions of small biological solutes

@article{Brady2011WeaklyHS,
  title={Weakly hydrated surfaces and the binding interactions of small biological solutes},
  author={John W. Brady and Letizia Tavagnacco and Laurent Ehrlich and M. -S. Chen and Udo Schnupf and Michael E. Himmel and Marie-Louise Saboungi and Attilio Ces{\`a}ro},
  journal={European Biophysics Journal},
  year={2011},
  volume={41},
  pages={369-377}
}
Extended planar hydrophobic surfaces, such as are found in the side chains of the amino acids histidine, phenylalanine, tyrosine, and tryptophan, exhibit an affinity for the weakly hydrated faces of glucopyranose. In addition, molecular species such as these, including indole, caffeine, and imidazole, exhibit a weak tendency to pair together by hydrophobic… CONTINUE READING