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Updated: May 27, 2026
Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Weakly hydrated surfaces and the binding interactions of small biological solutes
John W Brady1, Letizia Tavagnacco, Laurent Ehrlich
1Department of Food Science, Cornell University, Ithaca, NY 14853, USA. jwb7@cornell.edu
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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