LONG EXAM QUESTIONS Flashcards
Describe how DNA is replicated. [6 marks]
1~ DNA HELICASE attaches onto DNA molecule & breaks HYDROGEN BONDS between complementary bases.
2~ Each DNA strand acts as a TEMPLATE as 2 polynucleotide strands separate.
3~ FREE nucleotides form H bonds with complementary bases on DNA strand.
4~ DNA POLYMERASE catalyses formation of PHOSPHODIESTER bonds between adjacent nucleotides in condensation reaction.
5~ Forms 2 sets of DAUGHTER DNA helixes that have 1 parent (original) & 1 newly synthesised strand.
Relate the structure of a DNA molecule to its function. [6 marks]
Double helix structure w/ many H bonds =
Provides stability to molecule.
Coiling =
Makes DNA compact - stores lots of info in a small space.
Long molecule =
Stores a large amount of info.
Strong covalent sugar-phosphate backbone =
Gives strength - prevents code from being corrupted.
H bonds between bases are weak =
Allows chains to split easily for replication and transcription.
Sequence of bases =
Allows info to be stored.
Describe the structure and function of starch
Polymer of α-glucose.
Energy source and storage found in plants.
Insoluble = doesn’t affect water potential (no osmosis)
Large = doesn’t diffuse out of cells.
Made from AMYLOSE and AMYLOPECTIN
Describe the features of amylose
Polymer of α-glucose.
Forms ONLY 1-4 glycosidic bonds.
Helix and unbranched structure.
Compact.
Describe the features of amylopectin.
Polymer of α-glucose.
Forms BOTH 1,4 & 1,6 glycosidic bonds.
Helix and branched structure.
Compact.
Describe the structure and functions of glycogen.
Polymer of α-glucose.
Main energy source / storage in animals.
Forms BOTH 1,4 & 1,6 glycosidic bonds.
Branched structure.= many terminal ends for hydrolysis to glucose
Insoluble = doesn’t affect water potential
Large = doesn’t diffuse out of cells.
Compact = large energy release.
Describe the structure and function of cellulose.
Polymer of β-glucose.
Found in plant cell walls.
A structural unit = gives rigidity to plant cell walls (prevents bursting & holds stem up)
Hydrogen bonding between adjacent chains is found.
ONLY 1,4 glycosidic bonds
Straight-chain, unbranched structure
Alternate glucose molecules are rotated 180°
Forms microfibrils! = high tensile strength
Describe the Benedict’s test for non-reducing sugars.
Negative result: Benedict’s reagent remains blue.
1~ Add 1cm³ of dilute HCl and boil in water bath for 5mins.
2~ Neutralise mixture with sodium hydrogen carbonate solution.
3~ Proceed with Benedict’s test.
If positive: contains non-reducing sugars.
Describe the test for starch.
1~ Place food sample on spotting tile
2~ Add few drops of iodine solution
Positive result: colour change from orange to blue-black.
Describe the lipid (emulsion test)
1~ Place food sample in test tube.
Add 3cm³ of ethanol.
2~ Shake lidded tube thoroughly to dissolve any lipid in sample.
3~ Add 3cm³ of water and shake gently.
Positive test: solution turns cloudy (white emulsion forms)
How do you prepare a food test?
1~ Grind the food sample with a pestle and mortar while adding distilled water to help dissolve.
2~ Filter the food sample and collect the food sample solution.
3~ Place liquid into a test tube.
Relate the structure of triglycerides to their functions.
Non-polar molecule = hydrophobic = insoluble
no affect on water potential (used for waterproofing)
Releases a lot of ENERGY =
High number of C & H atoms - good storage and source of water via respiration.
LARGE = makes it good storage molecule.- can’t leave cell
Slow conductor of heat = (thermal insulation)
Less dense than water = (buoyancy of aquatic animals)
Relate the structure of phospholipids to their functions.
Amphipathic molecule =
Glycerol backbone attached to 2 HYDROPHOBIC fatty acid tails & 1 HYDROPHILIC phosphate head.
Amphipathic = forms phospholipid bilayer in water =
makes up cell membranes
Tails can splay outwards =
waterproofing
How do you test for proteins in a food sample?
Biuret test confirms presence of peptide bonds,
1~ Add equal volume of NaOH to sample at room temp.
2~ Add drops of dilute copper (II) sulfate solution.
Swirl to mix.
Positive result: colour change - blue to purple.
Negative result: solution remains blue.
Steps 1 & 2 make Biuret reagent.
What is the induced fit model of enzyme action?
1) Enzyme BINDS onto substrate.
2) Tertiary structure of the active site changes and becomes COMPLEMENTARY
3) It MOULDS itself tightly around the substrate - ensures the active site fits PERFECTLY
4) Temporary BONDS are formed - helps catalyse reaction
5) Bonds are STRESSED and products are formed.
Compare the lock & key theory with the induced-fit model.
Lock & key theory =
Active site doesn’t change shape when substrate binds.
Induced-fit model =
Tertiary structure of enzyme changes as substrate approaches so active site moulds around substrate.
Describe the effect of pH on the rate of reaction.
As the pH moves away from the optimum, the rate decreases.
Bc change in pH changes the CHARGES on the R groups of amino acids. Since H+ ions are donated.
So it changes the IONIC and HYDROGEN bonding between R groups.
Tertiary structure of active site changes, and enzyme has DENATURES.
Active site can no longer become complementary to substrate.
Fewer ES complexes formed.
Explain the effect of temperature on the rate of reaction.
Increase in temperature increases kinetic energy of molecules - move around more quickly and collide more frequently - more ES - complexes formed - rate of reaction increases.
At higher temperatures, hydrogen / other bonds in enzyme begin to break - changes tertiary structure to change - active site changes - substrate no longer fits in site - enzyme denatured - doesn’t function again.
OPTIMUM temp usually 40 degrees.
Describe the effect of enzyme concentration on the rate of reaction.
Given that substrate is in excess, rate increases proportionally to enzyme concentration.
Higher enzyme concentration means that more enzymes are available for ES complexes to form, more frequent successful collisions, increasing the rate.
Rate levels off when the maximum number of ES complexes form - when substrate is limiting.
Describe the effect of substrate concentration on the rate of reaction.
Given that enzyme concentration is fixed, rate increases proportionally to substrate concentration.
Higher substrate concentration means that more substrates are available for ES complexes to form, more frequent successful collisions, increasing the rate.
Rate levels off when the maximum number of ES complexes form - when enzymes are limiting.
Describe the structure of proteins [6 marks]
> Polymer of amino acids
Joined by peptide bonds
That are formed by condensation
> Primary structure is the sequence/order of amino acids
> Secondary structure is folding of polypeptide chain due to hydrogen bonding - forms alpha helixes / beta pleated sheets.
> Tertiary is 3D folding due to hydrogen, ionic and disulfide bonds.
> Quaternary structure is 2 or more polypeptide chains.
What is the role of ATP?
1~ ATP hydrolysis is exergonic, so there’s a release of free energy.
2~ Enzymes help couple the energy from ATP hydrolysis to endergonic reactions (which absorbs energy)
3~ The molecules in the endergonic are PHOSPHORYLATED and is more reactive than before.
4~ Molecules join together to form product, and Pi is produced (phosphate is removed).
5~ ATP is resynthesised as Pi joins to and ADP to form ATP.
What are the features of ATP?
A = amount of energy released is SMALL - can be coupled to energy-requiring reactions (endergonic) which don’t need too much energy - less energy wasted as heat.
T = ta da! Energy is released in a SINGLE reaction - very rapid, less time-consuming.
P = Pi (inorganic phosphate) released during ATP hydrolysis can be used to phosphorylate substances to make them MORE REACTIVE.
= Soluble =
Small & soluble so it can be easily transported around the cell.
= Cannot diffuse =
Can’t diffuse out of cell, meaning the cell will not run out of energy.
What are the advantages of hydrolysing ATP instead of glucose directly?
+ Energy is released very rapidly - only single bond broken, whereas in glucose a number of bonds are broken (which takes more time) - energetically more favourable.
+ Provides energy in small and usable amounts - glucose releases too much energy.