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AQA A Level Biology > 1A: Biological Molecules > Flashcards

1A: Biological Molecules Flashcards

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1
Q

The Theory of Evolution

A

All organisms on Earth are descended from one or a few common ancestors and that they have changed and diversified over time

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2
Q

Evidence for the Theory of Evolution

A

Universal DNA, same base sequences code for the same Amino Acids

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3
Q

Examples of Monomers

A

Monosaccharides, Amino Acids, Nucleotides

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4
Q

Examples of Polymers

A

Carbohydrates, Proteins, Nucleic Acids

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5
Q

Reaction to form Polymers from Monomers

A

Condensation Reaction

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6
Q

Reaction to break Polymers into Monomers

A

Hydrolysis

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7
Q

The elements in Monosaccharides

A

C, H, O

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8
Q

3 Examples of Monosaccharides

A

Glucose, Fructose, Galactose

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9
Q

Structure of Glucose

A

Hexose Sugar

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10
Q

Drawn Structure of Glucose

A

Alpha is same side for OH
Beta is opposite

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11
Q

3 Examples of Disaccharides

A

Sucrose, Lactose, Maltose

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12
Q

What Maltose is formed of

A

2 a-Glucose Molecules

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13
Q

What Lactose is formed of

A

Glucose and Galactose

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14
Q

What Sucrose is formed of

A

Glucose and Fructose

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15
Q

The name for the test for Sugars

A

Benedict’s Test

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16
Q

Steps to test for a Reducing Sugar

A
  1. Add Benedict’s Reagent and heat gently
  2. Positive result = Brick Red Precipitate. Negative result + Remain Blue
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17
Q

Steps to test for a Non-reducing Sugar

A
  1. Add Benedict’s Reagent and heat gently
  2. Negative result = remain blue
  3. Heat a new sample with dilute HCl
  4. Neutralise by adding Sodium Hydrogencarbonate
  5. Retest with step 1
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18
Q

Structure of Starch

A

Amylose- long, unbranched chain of a-Glucose coiled together compactly
Amylopectin- long, branched chain of a-Glucose, side chains are easily accessed by enzymes to help release Glucose quickly

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19
Q

Structure of Glycogen

A

Very branched chain of a-Glucose found in animals

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20
Q

Structure of Cellulose

A

long, unbranched chain of B-Glucose, chains held together by Hydrogen Bonds forming Microfibril Structure

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21
Q

Steps to test for Starch

A

Add Iodine dissolved in Potassium Iodide Solution. Positive result is orange to blue/black

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22
Q

Structure of a Triglyceride

A

1 Glycerol (hydrophilic) with 3 Fatty Acid Chains (hydrophobic)

23
Q

Difference between Saturated and Unsaturated fatty Acid

A

Unsaturated has a C=C double bond

24
Q

How Triglycerides are formed

A

Condensation Reactions to for Ester Bonds

25
Q

Structure of a Phospholipid

A

1 Glycerol (hydrophilic), 2 Fatty Acid Chains (hydrophobic), and a Phosphate Group

26
Q

Properties of Triglycerides

A

Used as energy storage molecules, long hydrocarbon tails can store lots of chemical energy
Insoluble in water, won’t affect water potential
Bundle into droplets

27
Q

Properties of Phospholipids

A

Can form a Bilayer, that is the cell membrane

28
Q

Test for Lipids

A

Emulsion Test
1. Shake substance with Ethanol
2. add water
Milky emulsion will form

29
Q

The monomer of Proteins

A

Amino Acids

30
Q

Structure of a Dipeptide

A

2 Amino Acids with Peptide Bond

31
Q

Structure of a Polypeptide

A

More than 2 Amino Acids joined together by Peptide Bonds

32
Q

Amino Acid Structure

A

A Carboxyl Group, an Amine Group, and an R Group

33
Q

Reaction to form Dipeptides and Polypeptides from Amino Acids

A

Condensation

34
Q

Structure of Proteins

A

Primary Structure- the sequence of Amino Acids in a Polypeptide Chain
Secondary Structure- Hydrogen Bonds form between Amino Acids in the chain and an Alpha Helix or beta Pleated Sheet is formed
Tertiary Structure- Hydrogen Bonds, Ionic Bonds, and Disulfide Bridges (between Cystines) form further folding the structure
Quaternary Structure- Multiple polypeptide chains held together by bonds

35
Q

Enzyme Structure

A

Roughly Spherical due to tight folding polypeptide chains
Soluble and often have roles in Metabolic Reactions

36
Q

Antibody Structure

A

Made of 2 light Polypeptide Chains
Have Variable Regions where the Amino Acid Sequence varies

37
Q

Transport Protein Structure

A

Contain Hydrophobic and Hydrophilic amino acids, which cause the proteins to fold up and form channels

38
Q

Structural proteins Structure

A

Physically Strong
Consist of long peptide chains lying parallel to each other with cross-links between them
eg. Keratin, collagen

39
Q

Steps to test for proteins

A
  1. add a few drops of Sodium Hydroxide Solution
  2. add some Copper (II) Sulfate solution
  3. positive result = Blue to Purple
40
Q

Definition of an Enzyme

A

Biological Catalyst

41
Q

How enzymes speed up reactions

A

Provide an alternate reaction pathway with lower activation energy

42
Q

When a substrate fits into an enzyme’s active site

A

Enzyme-Substrate Complex

43
Q

The Lock and Key Model

A

Enzyme is the lock, Substrate is the Key (wrong)

44
Q

The Induced Fit Model

A

Helps explain why Enzymes are so specific and only bond to one particular substrate
The active site changes shape to fit the substrate

45
Q

The factors affecting Enzyme Activity

A

Temperature, pH, Substrate Concentration, Enzyme Concentration

46
Q

Ways to measure enzyme activity

A
  1. How fast the product is made
  2. How fast the product is broken down
47
Q

How temperature affects enzyme activity

A

More heat = more kinetic energy = molecules move faster
This makes the substrate molecules more likely to collide with enzyme’s active site
If the temperature gets too high, the enzyme’s molecules vibrate more and this can break the bonds that hold the enzyme’s shape and cause it to denature

48
Q

How pH affects enzyme activity

A

al enzymes have an optimum pH
any pH other than this then the H+ and OH- ions in acids and alkalis disrupt the ionic bonds in the enzyme’s structure and cause it to denature

49
Q

How Substrate Concentration affects enzyme activity

A

the higher the substrate concentration, the faster the reaction (more successful collisions)
increases until saturation is reached

50
Q

How Enzyme Concentration affects enzyme activity

A

the higher the enzyme concentration, the faster the reaction (more successful collisions)
increases until saturation is reached

51
Q

Definition of Competitive Inhibitor

A

Has a similar shape to substrate molecule so takes its place, preventing other substrate molecules from bonding

52
Q

Definition of Non-competitive Inhibitor

A

Binds to allosteric site and changes shape of enzyme’s active site

53
Q

RP1- investigating enzyme-controlled reactions

A

Measuring rate of product production

  1. Set up boiling tubes containing the same volume and concentration of hydrogen peroxide
  2. To keep pH constant, add equal volumes of a suitable buffer solution to each boiling tube
  3. Set up the rest of the apparatus as shown in the diagram
  4. Put each boiling tube in a water bath set to a different temperature (10, 20, 30, 40) along with anopther tube containing catalase. Leave them for 5 minutes to get them to the correct temperature
  5. Use a pipette to add the same volume and concentration of catalase to each boiling tube. Then quickly attach the bung and delivery tube
  6. Record how much oxygen is produced in the first minute of the reaction
  7. Repeat the experiment at each temperature and use the results to find the mean volume of oxygen produced
  8. Calculate the mean rate of reaction at each temperature by dividing the volumes of oxygen produced by the time taken

Measuring the rate of substrate usage

  1. Put a drop of iodine in potassium iodide solution into each well on a spotting tile. Label the wells to help read the results
  2. Mix together a known concentration and volume of amylase and starch in a test tube
  3. Using a dropping pipette, put a drop of this mixture into one of the well containing iodine solution at regular intervals
  4. Observe the resulting colour change
  5. Record how long it takes for the iodine solution to no longer turn blue/black when the starch/amylase mixture is added
  6. Repeat the experiment using different concentrations of amylase
  7. Repeat 3x each time to calculate a mean time taken

AQA A Level Biology (10 decks)

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