Weakly hydrated surfaces and the binding interactions of small biological solutes |
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Authors: | John W Brady Letizia Tavagnacco Laurent Ehrlich Mo Chen Udo Schnupf Michael E Himmel Marie-Louise Saboungi Attilio Cesàro |
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Institution: | 1.Department of Food Science,Cornell University,Ithaca,USA;2.Department of Life Sciences,University of Trieste,Trieste,Italy;3.Centre de Recherche sur la Matière Divisée,Orléans,France;4.National Renewable Energy Laboratory,Golden,USA |
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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. |
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