Macromolecules of Life

Dr Chiaka Anumudu
Office B5
chiaka.anumudu@mail.ui.edu.ng
Chemistry is the logic that underlies
biological phenomena
Distinctive properties of living
systems
• Organisms are complicated and highly organised

• Biological structures serve functional purposes

• Living systems are actively engaged in energy

transformations

• Have a remarkable capacity for self replication

Biomolecules: the molecules of life
• H, O, C and N make up 99+% of the atoms ot the
human body.

• Question: What percentage does each element

contribute?
• Question: What is the rest??
• Question: What is the molecular composition of cells?
C, H, O and N form strong bonds with
each other
• Covalent bonds are made by sharing a pair of electrons

• Strongest type of bonds, about 80kcal/mol

• Fairly stable at room temp
• Single, c-c, double C=C, triple C=C

• Typical Covalent Bond Energies

Bond Energy kJ/mol
H-H 436
C-H 414
C-C 343
C-O 351
Covalent bonds
• There is free rotation about a single covalent bond, but not about a
double or triple bond.
• Covalent bonds also have a fixed angle.
• Some covalent bonds involve unequal sharing of electrons.
• Some atoms hold onto electrons more tightly than other atoms. The
tendency to attract electrons is a measure of electronegativity of an
atom.
Hydrogen bonds
• attraction between a slight positive charge on a hydrogen atom and a
slight negative charge on a nearby atom
• - strength of bond ~ 5 kcal/mol (relatively weak)
• - strongest when the donor, the hydrogen and the acceptor are about
0.25 nm apart
• - hydrogen bonds give order and structure to molecules
• - a single hydrogen bond is weak, however, most molecules are made
up of many
• hydrogen bonds; leads to overall strength of molecule
Ionic bonds
• electrostatic interaction between two oppositely charged groups in a
molecule
• limiting cause of unequal sharing of electrons; one atom keeps the
electron
• NaCl Na+ + Cl- unequal sharing of electrons, Cl keeps both
electrons
• In solution this group becomes ionized, loses a proton and becomes
negatively charged
Van der Waal’s interactions
• nonspecific attractive force that occurs when any two atoms come in
close range
• - most favourable when atoms are 0.2-0.3 nm apart
• - transient polarity induced between atoms a nonpolar bond leads to
attraction with nearby atoms
• - very weak interaction – strength is ~1 kcal/mol. However the sum of
many Van Der Waals interactions leads to increased strength and
stability
• Example: A ligand interacting with its receptor is accomplished by
many noncovalent interactions such as Van Der Walls interactions.
Hydrophobic interactions
• A molecule forms a particular shape because it likes to adopt the
lowest energy state (minimize entropy)
• groups that cannot form hydrogen bonds with water (the
hydrophobic ones) tend to cluster on the inside of the molecule (away
from water).
• Hydrophobic: (“water hating”) uncharged, nonpolar molecules, don’t
interact with water
• Hydrophilic: (“water loving”): charged or polar molecules; from
hydrogen bonds with water
The shape that a biological
macromolecule adopts is dependent on a
large number of molecular interactions

Covalent bonds give a wealth of

shapes in 3D
 And a wealth of functionality
DNA
• C=O and N-H functionalities
– H-bond acceptors and
donors
• Covalent bonds make the
backbone and the bases
(A,C,G,T)
• H-bonds dictate the register
and direction
– A:T
– G:C
– antiparallel
A biomolecular hierarchy
Simple molecules are the units for
building complex structures

• Metabolites and macromolecules

• Organelles
• Membranes
• The Cell
Properties of biomolecules reflect
their fitness for life
Chiral monomers make complex
biopolymers
Back to our weak bonds….
• What is the energy (strength) of the weak bonds:

• hydrogen bond=
• ionic bond=
• van der walls =
• hydrophobic interactions=
So weak bonds??
• Weak chemical forces mediate biomolecular recognition
• E.g.

• Restrict organisms to a narrow range of environmental conditions

• E.g.
Major Macromolecules I