2 Molecular Biology
2 Molecular Biology
2 Molecular Biology
2 Molecular Biology
2.1 Molecules to metabolism
Molecular biology:
● Reductionist approach in coming to conclusions. Can’t explain everything
by breaking down complex systems into small parts and studying them individually.
Need to study emergent properties as well, which only occur when the organisms
are studied as a whole.
Synthesis of Urea:
Vitalism:
● Origin of all life comes due to a “vital principle”, which is different to life
Carbon Compounds:
● Carbon atoms can form 4 covalent bonds. These can be single or double
bonds.
● Can form chains/rings of any length.
contain sulphur.
temperature and oils if liquid. Also contain Carbon Hydrogen and Oxygen.
Drawing molecules:
respectively.
o ● Amino Acids: Contain Amine group; Carboxyl group; Hydrogen atom; and
R variable group.
o ● Lipids contain less oxygen than carbohydrates. Proteins usually contain
sulphur. Carbohydrates have a H:O ratio of 2:1.
Metabolism:
anabolic process.
2.2 Water
Hydrogen bonding in water:
o ● Water molecules are polar and hydrogen bonds form between them.
o ● Bonds between hydrogen and oxygen involve the unequal sharing of
Water properties:
group. All amino acids, however, are soluble enough to dissolve in blood
plasma.
o ● In alpha glucose the OH points downwards and in beta, it points upwards.
o ● Cellulose: Linking beta glucose in a 1-4 structure makes cellulose. OH
Lipids:
glycerol.
(20 ̊C).
Triglycerides:
Energy storage:
carbohydrates.
o ● Adipose tissue is located directly beneath the skin and round some organs
carbohydrates.
o ● Fats store as pure droplets whereas glucose stores with two grams of
carbohydrates.
o ● Lipids are insulators as they are poor conductors of heat. This is why
o ● They can also act as shock absorbers because they are liquid at body
temperature.
o ● However fat cannot be rapidly used and therefore can only be used in
aerobic respiration.
Fatty Acids:
the double bond. If they are on opposite sides they are trans.
o In cid fatty acids there is a kink at the double bond, which causes the fatty acid to
bend. This contributes to cis’s ability to pack tightly in regular arrays; far more
efficiently stored than saturated
hydrogenated in a factory.
Health risks:
2.4 Proteins
Amino acids and polypeptides:
bases.
RIP BIO CLASS OF 2K17
o ● Lysozyme: 1 polypeptide.
o ● Integrin: 2 polypeptides.
o ● Collagen: 3 polypeptides.
o ● Haemoglobin: 4 polypeptides.
Protein conformations:
Fibrous Globular
Elongated, with a repeating Intricate shape with parts that are helical or sheet-
structure like.
Polypeptide folds up as amino acids are added on.
Have bonds between the R groups of the amino acids.
No folding up, amino acid
prevents it. Hydrophobic groups on the inside and hydrophilic
groups on the outside.
Denaturation of protein:
o ● Heat/pH extremes (causes).
o ● Bonds in 3D structure of protein are susceptible to breakage.
o ● This breakage in bonds results in denaturation.
o ● Denatured protein does not normally return back to its former structure.
Protein functions:
o ● Catalysis.
o ● Muscle contractions.
o ● Cytoskeletons.
o ● Tensile strengthening.
o ● Blood clotting.
o ● Transport of nutrients and gases.
o ● Cell adhesion.
o ● Membrane transport.
o ● Hormones and receptors.
o ● DNA packing.
o ● Immunity.
Examples of proteins:
● Rubisco: Ribulose phosphate carboxylase. Catalyses the reactions for
carbon fixation.
o ● Insulin: Signal to cells to absorb glucose. Reduces blood glucose. Shape and
chemical properties correspond to binding site on the receptor. Secreted by
beta cells in pancreas.
o ● Immunoglobulin: Antibody. Binding sites for bacterial antigens has a
different binding cite – specific immunity.
o ● Collagen: Rope-like protein made of three polypeptides wound together.
They are located in the skin, blood vessel walls to prevent tearing and allow
for tensile strength.
o ● Rhodopsin: Pigments of rhodopsin, membrane proteins of rod cells in the
retina are light sensitive molecules surrounded by an opsin polypeptide.
Changes in shape when it absorbs light, triggers opsin and abuses the rod cell
to send an impulse to the brain.
o ● Spider silk: Polypeptide forms parallel arrays very resistant to breaking.
Proteomes:
organised is fixed but a proteome is not because different cells make different
proteins. Proteomes reveal what is happening in a cell at the time, not what could
happen. Proteomes differ due to differences in amino acid sequences.
2.5 Enzymes:
Active site and enzymes:
substrate only.
o ● Shape and chemical properties of active site and substrates match each
other.
● Collision: when enzyme and substrate come together. Collisions occur because of
random movements and are successful when the substrate and active site are
correctly lined up to each other.
pH: Enzymes have an optimum pH for functionality. Change in pH, or deviation from
the optimum pH, results in reduced rate of reaction. When
Immobilised enzyme:
o ● Advantages:
rate.
● Lactose free milk: Lactose is broken down into glucose and galactose with
o Nitrogenous base: Made of nitrogen. Either two/one rings of atoms in its structure
(purine (AG)/pyrimidine (CT)).
nucleotide and the sugar of the next - phosphate with no3 Carbon. o Creates a
backbone of alternating sugar and phosphate groups.
o Base sequence can vary, and this is how information is stored,
Structure of DNA:
o ● Double helix.
o ● Made of two antiparallel strands of nucleotides linked by hydrogen
other.
o ● Two strands are wound together to form a double helix and are held
together by hydrogen bonds between the nitrogenous bases. 2 hydrogen
DNA.
DNA Helicase:
o ● Unwinds the double helix and separates the two strands by breaking the
hydrogen bonds. Groups of enzymes that use energy from ATP are
as a template.
o ● Each of the two strands after helicase splits the DNA molecule, are used as
templates.
DNA RNA
Deoxyribose - 2nd Carbon has no hydroxyl
Ribose
group
Two polymers of nucleotides (double One polymer of nucleotide (single
stranded) stranded)
Thymine Uracil
existing end of a new strand. This is done by making covalent bonds between
the phosphate groups of the new nucleotide on the new strand the sugar
group of the existing nucleotide on the new strand.
sequence.
o DNA molecule is then cooled to 54 ̊C for 25 seconds during which multiple DNA
primase enzymes bind RNA primers bind on the parent strands. This stops them
from re-annealing with each other and also provides a starting point for replication.
o Reaction mixture then heated to 72oC, the temperature at which Taq DNA
polymerase works and adds complementary nucleotides to template strands.
o ● Synthesis of mRNA from the DNA base sequence using RNA polymerase.
o ● Proteins are what determine observable characteristics in an organism.
o ● Transcription occurs along the antisense strand. RNA polymerase binds
to it at the start of a gene and then moves along to separate the two DNA
strands. Concurrently it pairs RNA nucleotides with complementary bases.
Ribosomes:
a large subunit. Have binding sites for each molecule that partakes in the
process.
o ● Large subunit makes peptide bonds between amino acids to link the,
code.
required to be made.
Codons:
o ● Genetic code converts base sequence on mRNA into amino acid sequence.
o ● Sequence of three bases is called a codon. 64 possible codons.
o ● Genetic code is degenerate - many codons specify the same amino acid.
o ● Each amino acid is carried by a transfer RNA. Contains a 3 base anti-
codon complementary to the mRNA codon for that particular amino acid.
o ● Ribosomes act as the binding site for both mRNA and tRNA. They catalyse
assembly of polypeptide.
mRNA codon.
o 2nd tRNA binds. Maximum of two tRNA can be bound to a ribosome
at one time.
o Amino acids from first tRNA goes to second tRNA and joins by a
o ● Earlier bovine insulin was used. Despite slight genetic difference they still
Cell respiration:
the cell.
● ATP is used by splitting ATP into ADP + P. This is an exothermic reaction and
releases energy. This energy is used by cells and then converted into heat energy,
which is not reusable/recyclable. As a result all energy is eventually lost to the
environment, thus creating a continuous need to obtain energy through ingestion
and then respiration.
Anaerobic respiration:
o ● Gives a small yield of ATP from glucose, which is broken down without
oxygen.
environments.
o ● In humans, glucose is converted into lactic acid. However in yeast and
plants it converts to ethanol and carbon dioxide. Both lactate and ethanol are
toxic.
Use of yeast in baking:
texture in bread.
movements.
Aerobic respiration:
2.9 Photosynthesis:
Photosynthesis:
● Production of carbon compounds in cells using light energy.
Photosynthesis is an example of energy conversion. Light energy is converted to
chemical energy in carbon compounds. Produces carbohydrates, proteins and lipids.
Wavelengths of light:
o ● Visible light has a range of wavelengths with violet the shortest and red
different wavelengths.
100%.
away.
photosynthesis.
Production of Carbohydrates:
Limiting factors:
by controlling them. The third would be the independent variable and would
change by stead increments.
3 Genetics
3.1 Genes
What is a gene?
a specific characteristic.