TY - JOUR
T1 - Weakly Hydrated Surfaces and the Binding Interactions of Small Biological Solutes
AU - Brady, John W.
AU - Tavagnacco, Letizia
AU - Ehrlich, Laurent
AU - Chen, Mo
AU - Schnupf, Udo
AU - Himmel, Michael E.
AU - Saboungi, Marie Louise
AU - Cesáro, Attilio
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
KW - Hydrophobic hydration
KW - Molecular aggregation
KW - Molecular dynamics
KW - Serotonin
UR - http://www.scopus.com/inward/record.url?scp=84860312311&partnerID=8YFLogxK
U2 - 10.1007/s00249-011-0776-2
DO - 10.1007/s00249-011-0776-2
M3 - Article
C2 - 22124617
AN - SCOPUS:84860312311
SN - 0175-7571
VL - 41
SP - 369
EP - 377
JO - European Biophysics Journal
JF - European Biophysics Journal
IS - 4
ER -