Biological molecules Flashcards
Describe and explain 3 features of glycogen that make it well suited to its role as an energy store (6 marks)
- It is poorly soluble which means that it won’t affect water potential in cells
- It is compact which means it can fit into small storage granules
- It is easily synthesised and broken down which means that it rapidly responds to the hormones insulin and glucagon
Describe the structural differences between amylose and amylopectin and explain their effects on the starch molecule (4 marks)
Amylose contain 1,4 glycosidic bonds between monomers. These bonds cause amylose to form a compact coiled shape.
Amylopectin contains a mixture of 1,4 and 1,6 glycosidic bonds between monomers. The presence of these bonds results in a branched structure that allows folding for even more compactness.
Outline one structural similarity and one structural difference between amylopectin and glycogen (2 marks)
Similarity: they both have a combination of 1,4 and 1,6 glycosidic bonds
Differences: Glycogen has a much greater proportion of 1,6 glycosidic bonds compared to amylopectin.
Glycogen has a more compact structure
Give one similarity and one difference between the structures of glucose and fructose
(2 marks)
SIMILARITIES
- both are hexose sugars
- they have the same molecular formula
DIFFERENCES
- glucose is a 6 atom ring whereas fructose is a 5 atom ring
Describe 2 experimental methods by which the glycosidic bond in a disaccharide can be broken
(4 marks)
METHOD 1
Enzyme hydrolysis
Mix the disaccharide with the enzyme at room temperature
METHOD 2
Acid hydrolysis
Boil a sample with dilute hydrochloric acid
Explain the advantages of storing food as starch, rather than as sugars, in plant cells
(3 marks)
Starch is compact and highly branch
Starch is insoluble so does not have an effect of the water potential of the cell
Starch is easily broken down when needed
Describe a biochemical test for lipids
(2 marks)
Mix the sample with ethanol followed by water.
A milky white emulsion will form
Describe and explain the role played by bile and its component in the processing of lipids
(3 marks)
Bile emulsifies lipids by bile slats attaching to lipids and turning them into smaller droplets.
Bile salts form micelles with the the hydrolysis product of triglycerides. Micelles transports monoglycerides to the outer surface of the intestinal epithelium for absorption
Describe the differences between phospholipids and triglycerides
(2 marks)
Phospholipids have 2 fatty acids and are also bonded to a phosphate group
Explain how the secondary structure of a protein contributes to its overall 3D shape
(4 marks)
Due the hydrogen bonding between the amine and carboxyl groups of separate amino acids, every 4 amino acids along the chain the protein forms a alpha helix. A beta pleated sheet forms by folding the chain back on itself. Both structures provide bulk to the protein.
Describe the quaternary structure of haemoglobin and explain how its structure relates to its function in mammals
(6 marks)
STRUCTURE
A quaternary structure is 4 separate polypeptide chains bonded together. Each polypeptide chain is bonded to a haem group which contains an iron ion.
BENEFITS TO FUCNTION
The function of haemoglobin is to bind to oxygen in the lungs and release oxygen at respiring tissue. The binding of oxygen to one haem group increases the affinity of haemoglobin for oxygen. By changing the shape of the whole protein haemoglobin can deliver oxygen readily to the tissues that require it the most.
Describe the biochemical test for proteins
(2 marks)
Mix the solution with Biuret reagent. A positive result will produce a purple solvent.
Explain the induced fit hypothesis
(3 marks)
In the induced fit hypothesis:
- enzyme structure is not rigid
- the active site and substrate are not a perfect 3-D fit
- the active site changes shape to fit the substrate
- this can stress the substrate and weaken its bonds which lower the activation energy
Describe and explain 2 ways in which an enzyme can become denatured
(4 marks)
High temperatures
Extremes of pH
Both of these conditions cause the weak bonds in the tertiary structure to break whcih changes the shape of the active site.
Describe and explain the similarities and differences between competitive and non-competitive inhibitors
(6 marks)
SIMILARITIES
- the inhibitor binds to the enzyme’s surface
- there is a reduction in the enzyme’s rate
- the rate of initial reaction is inversely proportional to inhibitor concentration
DIFFERENCES
- competitive inhibitors bind to the active site and non-competitive inhibitors bind away from the active site
- in competitive inhibition the active site is blocked and in non-competitive inhibition the active site changes shape
- increasing substrate concentration will decrease the effect of competitive inhibition but will not affect non-competitive inhibition