1.1 General Properties and Types of Cells 1.

2 Introduction to Macromolecules
➔ All living organisms are composed of cells; ➔ Proteins -- amino acid -- peptide bond
Cells are the basic unit of life; Cells arise from
pre-existing cells
➔ A cell (1) has a stable blueprint of information
that self-replicates in the form of DNA (2) is
bounded by a semi-permeable plasma
membrane (3) uses metabolic processes to
harness, convert and use energy for cellular
processes
➔ Nucleic acid -- nucleotide -- phosphodiester
➔ Central Dogma: describes the basic flow of
bond
information in a cell
➔ Prokaryotes vs Eukaryotes
Prokaryotes Eukaryotes
With nucleus No nucleus (nucleoid)
No extensive internal Have membrane
compartmentalization bound organelles
Small surface area to Larger SA:V ratio
volume ratio

➔ Prokaryotes arose 3.5 billion years ago while ➔ Carbohydrate -- monosaccharide --

Eukaryotes arose 2 billion years ago glycosidic bond
➔ Biodiversity of cells: different shapes, different
sizes, multicellular of unicellular. Despite this,
all cells are still made up of the same
macromolecules and come from a common
ancestor
➔ Phylogenetic tree: Eukaryotes are closer to
archaea; bacteria have the most biodiversity
➔ Lipids -- fatty acids -- ester linkage (usually
among all domains
defined by hydrophobic properties) ; doesn’t
➔ Endosymbiotic theory: The endosymbionts
preserve polarity of its sub-units
(mitochondria & chloroplasts) once existed as
independent cells, but were engulfed by the
plasma membrane of early eukaryotes.
➔ Proof : Bacteria and chloroplasts were
membrane bound (from endocytosis),
endosymbionts were the same size as
bacteria, circular DNA similar to prokaryotes
1.3 Phospholipids, membrane structure, 1.4 Membrane selective permeability,
and membrane self assembly transport, diffusion, and osmosis
Micelles Lipids with bulky heads
and single tails
Bilayer Mixed lipids with small
heads and double tails
found in all cells
Liposomes Purified lipids with small
heads and double tails
Single Not possible due to
Sheets hydrophobic tails
➔ Osmosis: Diffusion of water across a
membrane from low solute to high solute
➔ Diffusion produces a net transport of
molecules from higher concentration to
lower concentration by random motion.
➔ Aquaporins: Channels that allow water to
move much more rapidly across membrane
➔ Osmosis: Net movement of a solvent across
a semipermeable membrane
➔ Osmotic pressure: Pressure that would
need to be applied to stop osmosis.
Pressure is applied to higher solute
concentration
➔ Energetically favourable: -ΔG
➔ Passive Transport (Diffusion) -- intrinsic
➔ Entropy > Enthalpy
energy of molecules
➔ Lipid molecules are able to move very
➔ Simple diffusion vs facilitated diffusion
rapidly because weak van der Waals forces
➔ Channel: Position is fixed; solute materials
are easily broken and reformed
diffuse through pores. Some channels are
➔ Longer fatty acid tail -- less fluid
gated. For ions and water soluble materials
➔ Unsaturated bonds -- more fluid
only. Facilitated diffusion.
➔ At temperatures found in a cell, cholesterol
➔ Carrier: Flips between two conformations;
decreases membrane fluidity bc it interacts
Usually for large, polar molecules (e.g.
with fatty acids
sugars and amino acids). Active transport
➔ At lower temperatures, it increases
and facilitated diffusion
membrane fluidity by preventing
➔ Active transport: Uses ATP (direct/indirect)
phospholipids from packing tightly
➔ Primary active transport: ATP directly
➔ Integral membrane vs peripheral
transports molecules. (3Na out ; 2K in)
➔ Fluid Mosaic Model: Fluid structure within
➔ Secondary active transport: Primary
which molecules move laterally + mosaic of
happens first to establish a concentration
lipids and proteins
gradient. Energy from electrochemical
➔ How? Fluorescent recovery after
gradient is used to transport another
photobleaching -- proteins were dyed and a
molecule. Proton moves from high to low
small spot on membrane was bleached.
concentration while coupled molecule
Results show that the bleached spot
moves from low to high concentration
became fluorescent over time as proteins
➔ Antiport vs. Symport
moved into bleached area.
 1.4 Membrane selective permeability, 1.5 Proteins: Structure and self‐assembly
transport, diffusion, and osmosis

➔ Animals keep their intercellular fluid isotonic ➔ Primary structure- sequence of amino acids.
with the extracellular fluid ➔ Sequence of amino acids (their properties
➔ Ways to maintain cell shape and order) determine protein structure and
1. Active transport can be used to function.
maintain intracellular solute ➔ Proteins are sequenced in N → C direction
concentration ➔ Peptide bond is more attracted to C=O
2. Cell wall: When turgor pressure from group. Peptide bond has characteristics of a
water moving in cell by osmosis double bond (shorter than a single bond; not
helps cells become rigid free to rotate)
3. Contractile vacuoles also help. They
take up excess water from inside the
cell and expel them outside to make
solution isotonic
4. Vacuoles: Absorbs water and
contributes to turgor pressure
➔ Plant cell wall: Cellulose (polymer of
glucose)
➔ Fungi cell wall: Chitin (polymer of sugars)
➔ Bacterial cell wall: Peptidoglycan (polymer
of amino acids and sugars)

➔ Secondary structure- α helix and β sheets.

➔ Alpha helix forms due to H-bonds along
peptide backbone
➔ Beta-sheets form due to H-bonds between
areas of the peptide backbone
➔ Tertiary structure- three-dimensional folded
structure. Determined by the sum of all
non-covalent interaction (& disulfide bonds)
➔ Quaternary structure- different polypeptide
chains interact with each other.
➔ Denaturation: when proteins are exposed to
different factors (heat/pH) which disrupt the
non covalent interactions and cause an
amino acid to lose its tertiary structure and
function
1.6 Proteins: Enzymes as reaction catalysts Bonds in Biology
➔ Enzymes are catalytic proteins with high
specificity
➔ Rate of chemical reaction: Amount of
product formed or reactant consumed over
time
➔
1. Binding of substrates trigger a
conformational change
2. Transition state becomes more
stable because there is less free
energy (lower activation energy)
3. Reaction is catalysed
4. Products are made and released
➔ Protein’s tertiary structure is important for
enzyme activity
- Amino acids that make the active
site are typically far apart and
require R-group interactions for them
to get closer and form the active site
➔ Enzymes speed up the reaction, but don’t
determine if spontaneous or not

➔ Competitive Inhibitor: Inhibitor forms a

complex with the active site to prevent
substrate from binding
➔ Non-competitive inhibitor: Binds to enzymes
at a different site than the active site
➔ Allosteric Enzymes: They bind to a place
other than the active site and cause
conformational, affinity or activity change.
➔ Positive feedback: When the product of the
reaction binds to enzyme at site other than
the active site to speed up the reaction
➔ Negative feedback: When the product of the
reaction binds to enzyme at site other than
the active site to slow down the reaction