title: Weakly hydrated surfaces and the binding interactions of small biological solutes.
abstract: 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.
authors: Department of Food Science, Cornell University, Ithaca, NY 14853, USA. jwb7@cornell.edu
authors: John W
authors: JW
authors: Brady
authors: Letizia
authors: L
authors: Tavagnacco
authors: Laurent
authors: L
authors: Ehrlich
authors: Mo
authors: M
authors: Chen
authors: Udo
authors: U
authors: Schnupf
authors: Michael E
authors: ME
authors: Himmel
authors: Marie-Louise
authors: ML
authors: Saboungi
authors: Attilio
authors: A
authors: Cesàro
mesh_terms: D005947:Glucose / Q000737:chemistry / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012997:Solvents / Q000737:chemistry*; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D012997:Solvents; D014867:Water; D005947:Glucose