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Title: Weakly Hydrated Surfaces and the Binding Interactions of Small Biological Solutes

Journal Article · · European Biophysics Journal

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.

Research Organization:
National Renewable Energy Laboratory (NREL), Golden, CO (United States)
Sponsoring Organization:
USDOE Office of Science, Biological and Environmental Research; USDOE Office of Energy Efficiency and Renewable Energy Biomass Program; National Institutes of Health (NIH)
DOE Contract Number:
AC36-08GO28308
OSTI ID:
1047952
Report Number(s):
NREL/JA-2700-55119; EBJOE8; TRN: US201216%%579
Journal Information:
European Biophysics Journal, Vol. 41, Issue 4; ISSN 0175-7571
Country of Publication:
United States
Language:
English

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