1) Biological Molecules Flashcards

1
Q

What is hydrolysis

A
  1. Breaks a chemical bonds between two molecules;
  2. Using water;
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2
Q

Structure of glycogen

A
  1. Polysaccharide of α-glucose;
  2. (Joined by) glycosidic bonds;
  3. Branched structure;
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3
Q

Compare glycogen molecule with cellulose

A

1) Cellulose is made up of β-glucose (monomers) and glycogen is made up of α-glucose (monomers);

2) Cellulose molecule has straight chain and glycogen is branched;

3) Cellulose molecule has straight chain and glycogen is coiled;

4) Glycogen has 1,4- and 1,6- glycosidic bonds and cellulose hxas only 1,4- glycosidic bonds

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4
Q

Structure of glycogen related to its function

A

1) Insoluble (in water), so doesn’t affect water potential;

2) Branched / coiled / (α-)helix, so makes molecule compact;

3) Polymer of (α-)glucose so provides glucose for respiration;

4) Branched / more ends for fast breakdown / enzyme action;

5) Large (molecule), so can’t cross the cell membrane

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5
Q

Structure of starch related to its function

A
  1. Insoluble - Don’t affect water potential;
  2. Helical - Compact;
  3. Large molecule - Cannot leave cell;
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6
Q

Phospholipids compared with
Triglycerides

A
  • Both contain ester bonds (between glycerol and fatty acid);
  • Both contain glycerol;
  • Fatty acids on both may be saturated or unsaturated;
  • Both are insoluble in water;
  • Both contain C, H and O but phospholipids also contain P;
  • Triglyceride has three fatty acids and phospholipid has two fatty acids plus phosphate group;
  • Triglycerides are hydrophobic/non-polar and phospholipids have hydrophilic/polar and hydrophobic/polar
    region;
  • Phospholipids form monolayer (on surface)/micelle/bilayer (in water) but triglycerides don’t;
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7
Q

Structure of protein

A
  1. Polymer of amino acids;
  2. Joined by peptide bonds;
  3. Formed by condensation;
  4. Primary structure is order of amino acids;
  5. Secondary structure is folding of polypeptide chain due to hydrogen bonding
    6.Tertiary structure is 3-D folding due to hydrogen bonding and ionic/disulfide bonds;
  6. Quaternary structure is two or more polypeptide chains;
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8
Q

Induced fit model of enzyme

A
  1. (before reaction) active site not complementary to/does not fit substrate;
  2. Shape of active site changes as substrate binds/as enzyme-substrate complex forms;
  3. Stressing/distorting/bending bonds (in substrate leading to reaction);
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9
Q

Increased temperature and reaction rate - enzymes

A
  1. particles have more kinetic energy
  2. therefore they move more
  3. so there are more collisions between substrates and active sites
  4. so more ES complexes form
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10
Q

Denaturation- enzymes

A
  1. Heat above the optimum breaks hydrogen bonds
  2. this causes the tertiary structure to unfold
  3. so the active site changes shape
  4. substrate can no longer bind to the active site, as it’s no longer complementary
  5. so fewer ES complexes form
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11
Q

Effect of Changes in pH on enzymes

A
  1. Ionic bonds holding tertiary structure break
  2. active site distorts and substrate no longer binds to active site
  3. charges on amino acids in active site affected
  4. fewer ES complexes form
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12
Q

Concentration of
Substrate - enzymes

A
  1. (Rate of) increase in concentration of product slows as substrate is used up OR High initial rate as plenty of substrate/more E-S complexes;
  2. No increase after 25 minutes/at end/levels off because no substrate left;
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13
Q

Describe and explain
the temperature graph of enzyme
rate

A
  1. Initial rate of reaction faster at 37 °C (than 25 °C);
  2. Because more kinetic energy;
  3. So more E–S collisions/more E–S complexes formed;
  4. Graph reaches plateau /levels off at 37 °C;
  5. Because all substrate used up;
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14
Q

Comparison of
Competitive and Non Competitive
Inhibition

A
  1. Competitive inhibitor binds to active sites of enzyme but non-competitive inhibitor binds at allosteric site/away from active site;
  2. (Binding of) competitive inhibitor does not cause change in shape of active site but (binding of) non-competitive does (cause change in size of active site);
  3. So with competitive inhibitor, at high substrate concentrations (active) enzyme still available but with non- competitive inhibitor (active) enzymes no longer available;
  4. At higher substrate concentrations likelihood of enzyme-substrate collisions increases with competitive inhibitor
    but this is not possible with non-competitive inhibitor;
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15
Q

Effect of temperature linked to plant growth - enzymes

A

(As temperature increases,)

  1. Enzyme activity reduced/(some) enzymes denatured;
  2. Less photosynthesis, so fewer sugars formed (plants only);
  3. Less (complex) biological molecules/organic substances made (that add to mass);
  4. Less respiration;
  5. Less energy/ATP for growth;
  6. Less energy for named function associated with growth (eg mitosis)
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16
Q

What is DNA replication

A

1.Helicase unzips DNA double helix
2. by breaking hydrogen bonds
3. free DNA nucleotides in the nucleus complementary base pair OR A to T and C to G;
4. with exposed bases on both strands
5. hydrogen bonds between complementary base pairs reform
6. both strands act as a template
7. DNA polymerase (causes);
Nucleotides to join together (to form new strand)/phosphodiester bonds to form;

17
Q

DNA Semi-Conservative Replication

A
  1. Idea of both original strands being copied/both are template strands;
  2. Each new DNA molecule consists of one original and one new strand of DNA;
18
Q

Uses and properties of ATP as an
energy source

A
  1. Releases relatively small amount of energy / little energy lost as heat;
  2. Releases energy instantaneously;
  3. Phosphorylates other compounds, making them more reactive;
  4. Can be rapidly re-synthesised;
  5. Does not leave cells;
19
Q

ATP Structure compared with
DNA nucleotide

A
  1. ATP has ribose and DNA has deoxyribose;
  2. ATP has 3 phosphates and DNA nucleotide has one phosphate;
  3. Base is always adenine in ATP and bases vary in DNA nucleotide (A,C,G or T);
20
Q

Properties that make water
important for organisms

A
  1. A metabolite in condensation/hydrolysis/photosynthesis/respiration;
  2. A solvent so (metabolic) reactions can occur;
  3. High heat capacity so buffers changes in temperature;
  4. Large latent heat of vaporisation so provides a cooling effect (through evaporation);
  5. Cohesion (between water molecules) so supports columns of water (in plants);
  6. Cohesion (between water molecules) so produces surface tension supporting organisms;
21
Q

Test for reducing sugar

A
  1. Heat with Benedict’s reagent (1);
  2. colour change from blue to brick-red
22
Q

Test for non reducing sugar

A

1.Heat with Benedict’s reagent and no colour change (1);
2. boil with dilute HCl and then neutralise with NaHCO3 (1);
3. re- heat with Benedict’s reagent and colour change from blue to brick-red (1)

23
Q

Test for starch

A
  • Add iodine in potassium iodide solution (1);
  • colour change from brown to blue-black (1)
24
Q

Test for protein

A
  • Add Biuret reagent to the sample (1);
  • colour change to lilac (1) (or lilac band appears)
25
Emulsion test - lipid
- Add ethanol and shake (1); - add water and goes milky (1)