Weakly Hydrated Surfaces and the Binding Interactions of Small Biological Solutes

John W. Brady, Letizia Tavagnacco, Laurent Ehrlich, Mo Chen, Udo Schnupf, Michael E. Himmel, Marie Louise Saboungi, Attilio Cesáro

Research output: Contribution to journalArticlepeer-review

16 Scopus Citations


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 stacking in aqueous solution. These interactions can be partially understood in terms of recent models for the hydration of extended hydrophobic faces and should provide insight into the architecture of sugar-binding sites in proteins.

Original languageAmerican English
Pages (from-to)369-377
Number of pages9
JournalEuropean Biophysics Journal
Issue number4
StatePublished - 2012

NREL Publication Number

  • NREL/JA-2700-55119


  • Hydrophobic hydration
  • Molecular aggregation
  • Molecular dynamics
  • Serotonin


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