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Polarity (of water)
Uneven charge distribution caused by bent shape and oxygen's high electronegativity; gives water its dipole moment.
Hydrogen bond
Weak electrostatic attraction between a slightly positive H (on O or N) and a slightly negative O or N; gives water its cohesive properties.
Cohesion
Attraction between water molecules due to hydrogen bonding; responsible for surface tension and transpiration pull.
Adhesion
Attraction between water molecules and polar surfaces (e.g., xylem walls); assists capillary action in plants.
Specific heat
Amount of heat required to raise 1g of a substance by 1°C; water's high value buffers temperature changes.
Heat of vaporization
Energy needed to convert liquid to gas; water's high value makes evaporative cooling (sweating) effective.
Density anomaly of water
Ice is less dense than liquid water due to an open H-bond crystal lattice; ice floats, insulating aquatic ecosystems.
Hydration shell
A layer of water molecules surrounding a solute ion or polar molecule, oriented by partial charges to dissolve the solute.
Hydrophilic
Water-loving"; describes polar or charged molecules that readily dissolve in water.
Hydrophobic
Water-fearing"; describes nonpolar molecules that are poorly soluble and tend to aggregate in water.
Hydrophobic effect
Entropy-driven aggregation of nonpolar molecules in water; caused by the release of low-entropy clathrate cage water
Clathrate cage
Ordered, ice-like water structure encasing a nonpolar molecule; its low entropy makes nonpolar dissolution unfavorable.
Entropy (ΔS)
Measure of disorder; the hydrophobic effect is driven by a large increase in water's entropy upon cage release.
Amphipathic
A molecule containing both hydrophilic (polar) and hydrophobic (nonpolar) regions; e.g., phospholipids, bile salts.
Phospholipid bilayer
Spontaneously formed double layer of amphipathic phospholipids in water; hydrophobic tails inward, heads outward. Basis of cell membranes.
Micelle
Spherical amphipathic aggregate with hydrophobic core and hydrophilic surface; formed by detergents and fatty acid salts via the hydrophobic effect.
Protein folding (hydrophobic driving force)
Spherical amphipathic aggregate with hydrophobic core and hydrophilic surface; formed by detergents and fatty acid salts via the hydrophobic effect.
Gibbs free energy equation
ΔG = ΔH – TΔS; a reaction is spontaneous when ΔG < 0. Hydrophobic aggregation is driven by a large positive ΔS term.