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Edexcel Unit 1 The Nucleic Acids PDF
Edexcel Unit 1 The Nucleic Acids PDF
2
Semi-conservative DNA replication
1)Two single strands of the DNA molecule unzip along the line of hydrogen bonds by DNA helicase.
2) Each revealed parent strand acts as a template for a new strand to synthesise.
3)The exposed bases of the parent strand attract free mononucleotides to join each template via
complementary base pairing. The enzymes DNA polymerase and DNA ligase join the nucleotides
together with hydrogen bonds through condensation reactions to form new DNA strands.
4)The result is two new strands of DNA identical with the original piece. The new molecules
automatically coil up into the double helix.
Protein synthesis
RNA is closely related to DNA but it doesnt form complex molecules. The sequence of bases along a
strand of RNA is related to the sequence of bases on a small part of DNA in the nucleus different
types of RNA take different roles in the process of protein synthesis.
Messenger RNA (mRNA) carries information from the DNA in the nucleus out into the cytoplasm. It
is formed when a smell length of the DNA double helix unzips. The coding or antisense strand of the
DNA acts as a template for the formation of the mRNA. The mRNA then moves out of the nucleus
transporting the instruction from the genes to the surface of the ribosomes which are the site of
protein synthesis.
Transfer RNA (tRNA) is found in the cytoplasm it picks up particular amino acids from the vast
numbers always free there. The tRNA molecules each carrying an amino acid line up alongside the
mRNA on the surface of the ribosome building up a long chain of amino acids. Peptide links are
formed between the amino acids, joining them together to form a polypeptide chain which in turn
can be used to form a larger protein.
1) DNA is transcribed to give a length of mRNA
2) tRNA in the cell attaches to specific amino acids
2a) mRNA moves out of the nucleus and becomes engulfed by a ribosome
3) tRNA molecule carrying amino acid lines up against matching mRNA on the ribosome
4) Peptide links are formed between the amino acids brought by the tRNA
5) When the polypeptide is released into the cytoplasm, the tRNA units also unbind and return to
the cytoplasm to pick up more amino acids. The ribosome may read the mRNA again.
In protein synthesis the information held in the sequence of bases in a gene is translated into a
sequence of amino acids in a polypeptide chain.
Revision - Enzymes
Biological catalysts
A catalyst is a substance that speeds up a chemical reaction without being used up in the reaction
itself. In this sense, they only change the rate of reaction and not the products. They have high
molecular activity/ turnover number small quantity of enzyme can affect many molecules.
1 They catalyse metabolic reactions in our bodies (catabolic breakdown / anabolic build up)
2 Enzyme action can be intracellular or extracellular
3 They are globular proteins
4 They have a level of specifity due to their 3D shape the active site has a particular shape for
certain substrate molecules to bind to.
Activation energy
- Activation energy amount of energy required for chemicals before reaction can start (heat)
- Enzymes lower activation energy reactions happen at lower temperatures
Enzyme-substrate complex lowers activation energy - If two substrate molecules need to be joined, being attached to the enzyme holds them close
together reducing any repulsion between the molecules so they can join more easily.
- If the enzyme is catalysing a breakdown reaction, fitting into the active site puts strain on bonds in
the substrate so the substrate molecule breaks up more easily.
Lock and key substrate fits into the enzymes active site specific shapes for each
Induced fit enzyme and substrate have to fit together in the first place enzyme-substrate
complex changes shape slightly to complete the fit locking the substrate more tightly to the
enzyme. The substrate also has to make the active site change shape in a particular way.
Immobilized enzymes
- packed into columns and used over long periods
- higher temperatures can be used thermal stability
- high operating temperatures increase rate of reaction
- product doesnt have to be separated from enzyme saves money
- reusability
Enzyme experimentsMeasuring the initial rate of an enzyme-controlled reaction / repeat it / exponential / correlation
Measure how fast the product of the reaction appears
Catalase > hydrogen peroxide
- state what variables are controlled
- measure how much oxygen is given off in a gas cylinder
- different concentrations of enzyme (state them 10%, 20% etc.)
- measure the amount of oxygen given off after certain time period e.g. 1 min
- divide the volume of oxygen produced by the time initial rate of reaction
- more given off in first minute faster initial rate of reaction.
Rate of reaction
Affected by enzyme concentration
- More enzyme molecules more likely a substrate molecule will collide with one and form an
enzyme-substrate complex.
- If the amount of substrate is limited there comes a point when there are more than enough
enzyme molecules to deal with all the available substrate, so adding more enzymes has no further
effect.
Affected by substrate concentration
The enzyme can become saturated all of the active sites are occupied by substrate molecules and
a further increase in substrate concentration will not increase the reaction further. This point is
called v-max which is the maximum rate of reaction.
Temperature
Higher temperature more kinetic energy > more heat energy more collisions rate of reaction
increases. Optimum temperature enzymes catalytic activity is greatest (37.5) in humans. Above
this level the enzyme structure begins to break down (denature) (third/fourth structures unravel)
High levels - molecular bonds break down in protein permanently altering active site rendering it
functionless. Exceptions thermophillic / temperature coefficient rate of reaction at (x+10) /
rate of reaction at x
pH level
A lower ph more acidic higher number of hydrogen to form bonds with enzyme protein structure
High ph alkaline less bonds form (both affect structure that holds 3D protein structure.
- alteration of intermolecular bonds in extremes can denature the active site making it functionless
- enzymes have an optimum pH range works most effectively
Inhibition
active site-directed: occupy active site to prevent substrate molecule from binding.
non-active site-directed: inhibitors that attach to other parts distorting its shape