Study Notes on Salts, Noncovalent Interactions, and the Hydrophobic Effect
Dissolving Salts
Dissolving NaCl increases entropy by transitioning from a crystal (ordered) to a liquid (disordered) state.
Solubility in Water
Methane (CH$4$) has low solubility in water compared to glycerol, ethanol, fructose, and MgCl$2$.
Noncovalent Interactions
Types:
Ionic (Coulombic) interactions: electrostatic interactions between charged species.
Hydrogen bonds: interactions between polar molecules.
van der Waals interactions: weak interactions, consist of attractive (dispersion) and repulsive (steric) components.
Hydrophobic Effect: ordering of water molecules around nonpolar substances.
Noncovalent interactions do not involve sharing of electrons.
Strength of Noncovalent Interactions
Relative Strength (kJ/mol) and Distance (nm):
Van der Waals: 0.4-4.0 kJ/mol, 0.4-0.7 nm
Hydrogen Bonds: 12-30 kJ/mol, 0.3 nm
Ionic Interactions: ~20 kJ/mol, <0.25 nm
Hydrophobic Interactions: varies
Biochemical Significance of van der Waals Interactions
Weak and reversible yet universal.
Important for steric complementarity and structural stability of macromolecules (e.g., DNA).
The Hydrophobic Effect
Involves interactions of nonpolar molecules in aqueous solutions.
Key in processes like protein folding and lipid micelle formation.
Does not result from direct forces between nonpolar molecules.
Entropy Considerations
Water surrounding nonpolar solutes exhibits lower entropy, causing low solubility of hydrophobic substances.
Amphipathic lipids in water lower the overall entropy when dispersed.
Aggregation of nonpolar portions leads to higher entropy as fewer water molecules are ordered.
Ligand Binding and the Hydrophobic Effect
Enzymes often have hydrophobic binding sites for substrates and ligands.
Removal of ordered water increases entropy, facilitating binding.
Substrate binding involves shape complementarity after water displacement.