Cells are capable of:

a) Self-replication.
b) Storing and transmitting information.
c) Maintaining selectively dierent environments
(transport; cell signalling and
compartmentalization).
d) Harnessing and transforming energy.

Cytoskeleton - Helps cells maintain their shape and

serves as a network of tracks for the movement of
substances within the cell.
With two chemically distinct ends, polymers can:

Polar Functional Groups

- maintain directionality (a similar end to end chemical
orientation of the molecule).
Solubility in aqueous environment. - ensure that polymerization only occurs in only one
Increased reactivity. direction (because each end reacts with the other).

Non-Covalent Bonds
a) Substantial number -
Determined by chemistry of the
molecule i.e. charge and bond
polarity.
b) Surface topography that
interacting surfaces to
approach each other closely - Cholesterol Membrane Proteins
complementary shapes.
Normal temp. - reduced Transporters
fluidity - ID-ID between Receptors
Spontaneous Assembly of Bilayer
ring and tails. Enzymes
a) Shape of phospholipids. Low temp. - increased Anchors - Cell structure and shape.
b) Amphipathic nature. fluidity - prevents tight
c) Hydrophobic eect. packing.

Dependent upon conc. and pH.

 Enthalpy of Bilayer Formation
Water - Decreases: PD-ID to fewer, but
stronger PD-PD.
Phospholipids - Increases: PD-ID to more,
but weaker ID-ID.

Entropy of Bilayer Formation

Water - Increases: More m.f. because of
fewer non-covalent interactions with
Hydrophobic Eect - Tendency of non-polar substances/groups to phospholipids.
aggregate away from water molecules, increasing the stability of a Phospholipids - Less m.f. because of more
system ( T S of water increases) by increasing the motional freedom non-covalent interactions.
of water.

Describing Transport Graphs

- Whether the relationship is linear with time.
- The rates of changes of the variables.
- Whether the membrane is more or less permeable to a
molecule.

Roles of Proteins
As enzymes.
For movement or locomotion e.g. the flagellum.
For transport e.g. active transport, facilitated transporters.
For structure or adhesion e.g. cytoskeleton proteins.
As signalling proteins.

Secondary Structure - Local 3D structure stabilized by hydrogen bonding in the backbone of the polypeptide.
Tertiary Structure - Overall 3D structure formed by folding of entire polypeptide, stabilized by interactions between R
groups (non covalent interactions and disulfide bonds) as well as interactions between R groups and the backbone
atoms. [multiple alpha helices and beta barrels (beta sheets twisted & coiled to form a closed structure) are tertiary]

Quaternary Structure - 3D arrangement of two or more polypeptides, interacting to form a protein complex
composed of multiple subunits.

Denaturation
pH - aects ionization state of ionic amino acids.
Temperature - heat breaks down non-covalent interactions.
Detergents - bind to protein and destabilize non-covalent interactions.

Amino Acid Substitutions

Charge/polarity of amino acids:
- Hydrophobic eect - Substituting a polar or non-polar A.A. in a homogeneous pair disrupts the hydrophobic eect.
Size of amino acids - influences whether non-covalent interactions will actually form and their strength.
Location within protein - influences spatial proximity.