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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Related Subjects
09 BIOMASS FUELS
59 BASIC BIOLOGICAL SCIENCES
71 CLASSICAL AND QUANTUM MECHANICS
GENERAL PHYSICS
AFFINITY
AMINO ACIDS
AQUEOUS SOLUTIONS
ARCHITECTURE
CAFFEINE
CHAINS
HISTIDINE
HYDRATION
PHENYLALANINE
PROTEINS
SEROTONIN
SOLUTES
TRYPTOPHAN
TYROSINE
hydrophobic hydration
molecular dynamics
molecular aggregation
serotonin
59 BASIC BIOLOGICAL SCIENCES
71 CLASSICAL AND QUANTUM MECHANICS
GENERAL PHYSICS
AFFINITY
AMINO ACIDS
AQUEOUS SOLUTIONS
ARCHITECTURE
CAFFEINE
CHAINS
HISTIDINE
HYDRATION
PHENYLALANINE
PROTEINS
SEROTONIN
SOLUTES
TRYPTOPHAN
TYROSINE
hydrophobic hydration
molecular dynamics
molecular aggregation
serotonin