2 | Water and Aqueous Solutions

2013 W. H. Freeman and Company

2013W.H.FreemanandCompany
 CHAPTER 2
Water and Aqueous
Solutions
Learning goals:
What kind of interactions occur between
molecules
Why water is a good medium for life
Why nonpolar moieties aggregate in water
How dissolved molecules alter properties of
water
How weak acids and bases behave in water
How buffers work and why we need them
How water participates in biochemical reactions
 Water is the medium for
life
Life evolved in water (UV protection)

Organisms typically contain 7090% water

Chemical reactions occur in aqueous milieu

Water is a critical determinant of the

structure and function of proteins, nucleic
acids, and membranes
 Structure of the Water
Molecule
Octet rule dictates that there are four electron
pairs around an oxygen atom in water
These electrons are in four sp3 orbitals
Two of these pairs covalently link two
hydrogen atoms to a central oxygen atom
The two remaining pairs remain nonbonding
(lone pairs)
Water geometry is a distorted tetrahedron
The electronegativity of the oxygen atom
induces a net dipole moment
Because of the dipole moment, water can
serve as both a hydrogen bond donor and
acceptor
 Hydrogen Bonds
Strong dipole-dipole or charge-dipole interaction that
arises between an acid (proton donor) and a base (proton
acceptor)
Typically 46 kJ/mol for bonds with neutral atoms,
and 610 kJ/mol for bonds with one charged atom
Typically involves two electronegative atoms (frequently
nitrogen and oxygen)
Hydrogen bonds are strongest when the bonded
molecules are oriented to maximize electrostatic
interaction
Ideally the three atoms involved are in a line
 Hydrogen Bonding in
Water
Water can serve as both
an H donor
an H acceptor
Up to four H-bonds per water molecule gives water
its
anomalously high boiling point
anomalously high melting point
unusually large surface tension
Hydrogen bonding in water is cooperative
Hydrogen bonds between neighboring molecules
are weak (20 kJ/mol) relative to the HO covalent
bonds (420 kJ/mol)
 Ice: Water in a
Solid State
Water has many different crystal
forms;
the hexagonal ice is the most
common

Hexagonal ice forms a regular lattice,

and thus has a low entropy

Hexagonal ice contains more hydrogen

bonds/water molecule
Thus, ice has lower density than liquid
 Water as a Solvent

Water is a good solvent for charged

and polar substances
amino acids and peptides
small alcohols
carbohydrates
Water is a poor solvent for nonpolar
substances
nonpolar gases
aromatic moieties
aliphatic chains
 Water dissolves many
salts
High dielectric constant reduces attraction
between oppositely charged ions in salt
crystal; almost no attraction at large (>
40 nm) distances
Strong electrostatic interactions between
the solvated ions and water molecules
lower the energy of the system
Entropy increases as ordered crystal
lattice is dissolved
 Physics of Noncovalent
Interactions
Noncovalent interactions do not involve sharing a pair
of electrons. Based on their physical origin, one can
distinguish between:
Ionic (Coulombic) Interactions
Electrostatic interactions between permanently charged
species, or between the ion and a permanent dipole
Dipole Interactions
Electrostatic interactions between uncharged, but polar
molecules
van der Waals Interactions
Weak interactions between all atoms, regardless of polarity
Attractive (dispersion) and repulsive (steric) component
Hydrophobic Effect
Complex phenomenon associated with the ordering of water
molecules around nonpolar substances
Examples of Noncovalent
Interactions
Importance of Hydrogen Bonds
Source of unique properties of water
Structure and function of proteins
Structure and function of DNA
Structure and function of polysaccharides
Binding of substrates to enzymes
Binding of hormones to receptors
Matching of mRNA and tRNA

Ibelievethatasthemethodsofstructuralchemistryarefurtherappliedto
physiologicalproblems,itwillbefoundthatthesignificanceofthehydrogenbond
forphysiologyisgreaterthanthatofanyothersinglestructuralfeature.
LinusPauling,TheNatureoftheChemicalBond,1939
Hydrogen Bonds: Examples
Biological Relevance of Hydrogen Bonds
 van der Waals
Interactions
van der Waals interactions have two
components:
Attractive force (London dispersion)
depends on the polarizability
Repulsive force (Steric repulsion)
depends on the size of atoms
Attraction dominates at longer distances
(typically 0.40.7 nm)
Repulsion dominates at very short distances
There is a minimum energy distance (van
der Waals contact distance)
 Origin of the London
Dispersion Force
Quantum mechanical origin
Instantaneous polarization by fluctuating
charge distributions
Universal and always attractive
Stronger in polarizable molecules
Important only at a short range
Biochemical Significance of
van der Waals Interactions
Weak individually
easily broken, reversible
Universal
occur between any two atoms that are near each
other
Importance
determines steric complementarity
stabilizes biological macromolecules (stacking in
DNA)
facilitates binding of polarizable ligands
 The Hydrophobic Effect
Refers to the association or folding of
nonpolar molecules in the aqueous solution
Is one of the main factors behind:
protein folding
protein-protein association
formation of lipid micelles
binding of steroid hormones to their receptors
Does not arise because of some attractive
direct force between two nonpolar
molecules
 Solubility of Polar and
Nonpolar Solutes

Why are nonpolar molecules poorly soluble in wat

Low solubility of hydrophobic
solutes can be explained by
entropy
Bulk water has little order:
high entropy
Water near a hydrophobic solute is highly
ordered:
low entropy

Low entropy is thermodynamically

unfavorable, thus hydrophobic solutes have
low solubility.
Water surrounding nonpolar
solutes has lower entropy
Origin of the Hydrophobic
Effect (1)
Consider amphipathic lipids in water
Lipid molecules disperse in the solution;
nonpolar tail of each lipid molecule is
surrounded by ordered water molecules
Entropy of the system decreases
System is now in an unfavorable state
 Origin of the Hydrophobic
Effect (2)
Nonpolar portions of the amphipathic molecule
aggregate so that fewer water molecules are ordered

The released water molecules will be more random

and the entropy increases

All nonpolar groups are sequestered from water, and

the released water molecules increase the entropy
further

Only polar head groups are exposed and make

energetically favorable H-bonds
Hydrophobic effect favors
ligand binding

Binding sites in enzymes and receptors

are often hydrophobic

Such sites can bind hydrophobic

substrates and ligands such as steroid
hormones

Many drugs are designed to take

advantage of the hydrophobic effect
 Affects of Solutes on
Properties of Water
Colligative Properties
Boiling point, melting point, and osmolarity
Do not depend on the nature of the solute,
just the concentration
Noncolligative Properties
Viscosity, surface tension, taste, and color
Depend on the chemical nature of the solute

Cytoplasm of cells are highly

concentrated solutions and have high
osmotic pressure
Osmotic Pressure
Effect of Extracellular
Osmolarity
 Ionization of Water
H+ + OH-
H2O
O-H bonds are polar and can dissociate
heterolytically
Products are a proton (H+) and a hydroxide ion
(OH)
Dissociation of water is a rapid reversible process
Most water molecules remain un-ionized, thus pure
water has very low electrical conductivity
(resistance: 18 Mcm)
The equilibrium is strongly to the left
Extent of dissociation depends on the temperature
 Proton Hydration
Protons do not exist free in solution.
They are immediately hydrated to form hydronium
(oxonium) ions.
A hydronium ion is a water molecule with a proton
associated with one of the non-bonding electron
pairs.
Hydronium ions are solvated by nearby water
molecules.
The covalent and hydrogen bonds are
interchangeable. This allows for an extremely fast
mobility of protons in water via proton hopping.
Proton Hopping
 Ionization of Water:
Quantitative Treatment
Concentrations of participating species in an
equilibrium process
are not independent but are related[H via
+ the-
][OH ]

H2O constant:
equilibrium H + OH
+ -
Keq=
[H2O]

Keq can be determined experimentally, it is 1.81016 M

at 25C.
[H2O] can be determined from water density, it is 55.5
M.
- 14 2
K w K eq [H 2 O] [H ][OH ] 1 10 M
Ionic product of water:
 What is pH?
pH is defined as the
pH = -log[H+] negative logarithm of the
hydrogen ion
concentration
Simplifies equations
K w [H ][OH - ] 1 10 14 M 2
The pH and pOH must
log[H ] log[OH - ] 14 always add to 14
In neutral solution, [H+] =
pH pOH 14 [OH] and the pH is 7
pH can be negative ([H+]
= 6 M)
pH scale is logarithmic:
1 unit = 10-fold
pH of Some Common Liquids
 Dissociation of Weak
Electrolytes:
Principle
O Keq O Weak electrolytes
H3C + H2O H 3C + H3 O+
OH O- dissociate only partially
in water.
K a K eq [H 2 O]
Extent of dissociation is
[H ][CH 3COO - ] 5
determined by the acid
Ka 1.74 10 M
[CH COOH] dissociation constant Ka.
3

[CH 3COOH] We can calculate the pH

[H ] Ka
[CH 3COO ] if the Ka is known. But
some algebra is needed!
 Dissociation of Weak
Electrolytes: Example
What is the final pH of a solution when 0.1
moles of acetic acid is added to water to a
final volume of 1L?
O O
H3C
Ka We assume that
H3 C + H +

OH O- the only source of

0.1xxx H+ is the weak
acid
[ x ][ x ]
Ka 1.74 10 5 M
[0.1 - x]
To find the [H+], a
x 2 1.74 10 6 1.74 10 5 x quadratic
x 2 1.74 10 5 x 1.74 10 6 0 equation must be
solved
x=0.001310,pH=2.883
 Dissociation of Weak
Electrolytes: Simplification

O O The equation can be

Ka
H3C H3C + H+ simplified if the
OH O- amount of dissociated
0.1xxx species is much less
0.1xx than the amount of
undissociated acid
[ x ][ x ]
Ka 1.74 10 5 M Approximation works
[0.1]
for sufficiently weak
x 2 1.74 10 6 acids and bases
Check that x < [total
x=0.00132,pH=2.880
acid]
 pKa measures acidity
pKa = log Ka (strong acid large Ka small pKa)
 Buffers are mixtures of
weak acids and their
anions (conjugate base)
Buffers resist change in pH

At pH = pKa, there is a 50:50 mixture of

acid and anion forms of the compound

Buffering capacity of acid/anion system is

greatest at pH = pKa

Buffering capacity is lost when the pH

differs from pKa by more than 1 pH unit
Acetic Acid-Acetate as a Buffer
System
Weak acids have different pKas
 HendersonHasselbalch
Equation:
Derivation
[H ][A - ]
HA
H+ + A- Ka
[HA]
[HA]
[H ] K a
+

[A - ]

[HA]
- log[H] -logK a log
[A-]

-
[A ]
pH pK a log
[HA]
 Biological Buffer Systems
Maintenance of intracellular pH is vital to all cells
Enzyme-catalyzed reactions have optimal pH
Solubility of polar molecules depends on H-bond donors and
acceptors
Equilibrium between CO2 gas and dissolved HCO3 depends on pH

Buffer systems in vivo are mainly based on

phosphate, concentration in millimolar range
bicarbonate, important for blood plasma
histidine, efficient buffer at neutral pH

Buffer systems in vitro are often based on sulfonic acids

of cyclic amines
HEPES HO
PIPES N N
CHES SO3Na
Water as a Reactant in
Biochemistry
Water bound to proteins is
essential for their function
Water bound to proteins is
essential for their function
Water bound to proteins is
essential for their function
 Chapter 2: Summary

In this chapter, we learned about:

The nature of intermolecular forces

The properties and structure of liquid water
The behavior of weak acids and bases in
water
The way water can participate in biochemical
reactions