Temperature dependence of hydrophobic interactions: A mean force perspective, effects of water density, and nonadditivity of thermodynamic signatures

2000 ◽  
Vol 113 (11) ◽  
pp. 4683-4700 ◽  
Author(s):  
Seishi Shimizu ◽  
Hue Sun Chan
Keyword(s):  
Temperature Dependence ◽  
Hydrophobic Interactions ◽  
Water Density ◽  
Thermodynamic Signatures

The Temperature-Dependence of Hydrophobic Association in Water. Pair versus Bulk Hydrophobic Interactions

1997 ◽  
Vol 119 (18) ◽  
pp. 4206-4213 ◽  
Author(s):  
Susanna Lüdemann ◽  
Roger Abseher ◽  
Hellfried Schreiber ◽  
Othmar Steinhauser
Keyword(s):  
Temperature Dependence ◽  
Hydrophobic Interactions ◽  
Hydrophobic Association

scholarly journals Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context

2017 ◽  
Vol 114 (51) ◽  
pp. 13345-13350 ◽  
Author(s):  
Erte Xi ◽  
Vasudevan Venkateshwaran ◽  
Lijuan Li ◽  
Nicholas Rego ◽  
Amish J. Patel ◽  
...  
Keyword(s):  
Self Assembly ◽  
Driving Forces ◽  
Hydrophobic Interactions ◽  
Density Fluctuations ◽  
Hydroxyl Groups ◽  
Water Density ◽  
Hydration Shells ◽  
Protein Mutants ◽  
Assembled Monolayers ◽  
Water Adhesion

Hydrophobic interactions drive many important biomolecular self-assembly phenomena. However, characterizing hydrophobicity at the nanoscale has remained a challenge due to its nontrivial dependence on the chemistry and topography of biomolecular surfaces. Here we use molecular simulations coupled with enhanced sampling methods to systematically displace water molecules from the hydration shells of nanostructured solutes and calculate the free energetics of interfacial water density fluctuations, which quantify the extent of solute–water adhesion, and therefore solute hydrophobicity. In particular, we characterize the hydrophobicity of curved graphene sheets, self-assembled monolayers (SAMs) with chemical patterns, and mutants of the protein hydrophobin-II. We find that water density fluctuations are enhanced near concave nonpolar surfaces compared with those near flat or convex ones, suggesting that concave surfaces are more hydrophobic. We also find that patterned SAMs and protein mutants, having the same number of nonpolar and polar sites but different geometrical arrangements, can display significantly different strengths of adhesion with water. Specifically, hydroxyl groups reduce the hydrophobicity of methyl-terminated SAMs most effectively not when they are clustered together but when they are separated by one methyl group. Hydrophobin-II mutants show that a charged amino acid reduces the hydrophobicity of a large nonpolar patch when placed at its center, rather than at its edge. Our results highlight the power of water density fluctuations-based measures to characterize the hydrophobicity of nanoscale surfaces and caution against the use of additive approximations, such as the commonly used surface area models or hydropathy scales for characterizing biomolecular hydrophobicity and the associated driving forces of assembly.

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