Journal
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
Volume 41, Issue 4, Pages 369-377Publisher
SPRINGER
DOI: 10.1007/s00249-011-0776-2
Keywords
Hydrophobic hydration; Molecular dynamics; Molecular aggregation; Serotonin
Categories
Funding
- National Institutes of Health [GM63018]
- DOE Office of Science, Office of Biological and Environmental Research, through the BioEnergy Science Center (BESC), a DOE Bioenergy Research Center
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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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