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Biology Y12 > Section 1:Biological Molecules > Flashcards

Section 1:Biological Molecules Flashcards

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1
Q

What is a monomer?

A

An individual molecule that makes up chains of individual molecules

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2
Q

What is a polymer?

A

When monomers join together to form long chains

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3
Q

Give three examples of monomers

A
  1. Monosaccharides
  2. Amino Acids
  3. Nucleotides
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4
Q

Give two examples of polymers

A
  1. Carbohydrates
  2. Proteins
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5
Q

Describe what a condensation reaction is

A

A reaction which produces a molecule of water when a new sub-unit is attached

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6
Q

Describe what a hydrolysis reaction is

A

The process of breaking the bonds that link the sub-units of a polymer using water

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7
Q

What are the monomers in carbohydrates?

A

Saccharides (sugars)

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8
Q

List four monosaccharides

A
  1. α-glucose
  2. β-glucose
  3. Fructose
  4. Galactose
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9
Q

What are maltose, sucrose and lactose formed from?

A

Maltose=α-glucose+α-glucose
Sucrose=α-glucose+fructose
Lactose=α-glucose+galactose

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10
Q

What type of reaction occurs between two monosaccharides and what bond forms?

A

A condensation reaction takes place
Glycosidic bond is formed

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11
Q

Are monosaccharides reducing sugars or
non-reducing sugars?

A

All reducing sugars are monosaccharides

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12
Q

Describe the test for reducing sugars

A

Add benedict’s reagent(equal volume to test sample) and place in a boiling hot water bath(80-90)
Orange colouration reducing sugar present

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13
Q

Describe the test for
non-reducing sugars

A
  1. Add benedict’s reagent and place in a hot water bath
  2. If the colour does not change add dilue HCl acid and place in hot water bath
  3. Add NaCO3, then benedict’s reagent
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14
Q

Describe how polysaccharides are formed

A

Many monosaccharides are joined/combined in a condensation reaction

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15
Q

Describe the test for starch

A

Add two drops of iodine solution, to the test sample
If starch is present the solution will turn blue-black

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16
Q

Give the name of three polysaccharides

A
  1. Starch
  2. Glycogen
  3. Cellulose
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17
Q

What is the main role of starch?

A

Energy storage

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18
Q

What monomer units is starch made up of?

A

α-glucose

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19
Q

Five points

Why is starch’s structure suitable for energy storage?

A
  1. Insoluble~don’t affect WP~water not drawn in by osmosis
  2. large and insoluble~doesn’t diffuse out of cells
  3. compact~stored in a small space
  4. when hydrolysed forms α-glucose ~easily transported and readily used in respiration
  5. branched form has many ends~each can be acted on simultaneously~glucose monomers released very rapidly
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20
Q

What is the structure of starch?

A

α-helix held together by hydrogen bonds

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21
Q

What two different polysaccharides is starch made up of?

A

Amylose and amylopectin

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22
Q

What is the main function of glycogen?

A

Storage in animals

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23
Q

Four points

Why is glycogen’s structure suitable for it’s funtion?

A
  1. insoluble~doesn’t affect WP~doesn’t cause water to enter by osmosis
  2. insoluble~doesn’t diffues out of cell
  3. compact~can be stored in a small space
  4. more highly branched then starch~more ends to be simultaneously acted on by enzymes~more rapidly broken down to form glucose molecules~needed as animals have higher metabloic rates
24
Q

Why is cellulose different to glycogen and starch?

A

Cellulose is made up of monomers of β-glucose

25
Q

What is the structure of cellulose?

A

Straight,unbranched chains. Hydrogen bonds forms cross-links between adjacent chains
Adjacent glucose molecules rotated by 180 degrees

26
Q

What is the main role of cellulose?

A

To provide support and rigidity

27
Q

Three points

Why is cellulose’s structure suited to its function?

A
  1. made up of β-glucose molecules~so form long straight,unbranched chains
  2. cellulose chains run parallel to each other+cross-linked by HB~add collective strength
  3. molecules grouped to form microfibrils which group together to form fibrils~provides more strength
28
Q

Four points

What are the main roles of lipids?

A
  • Source of energy
  • Waterproofing
  • Insulation
  • Protection
29
Q

What is the difference between saturated and unsaturated fatty acids?

A

Saturated fatty acids means that the carbon atoms are linked to as many possible number of hydrogen atoms (contains no double bonds)

30
Q

Describe the test for lipids

A
  1. Add ethanol to the test sample,then water
  2. Gently shake the test tube
    A milky-white emulsion indicates the presences of lipids
31
Q

What are the two types of lipids?

A

Phospholipids and triglycerides

32
Q

Describe the structure of triglycerides

A

One glycerol and three fatty acid chains
Each fatty acid forms an ester bonds with the glycerol in a condensation reaction

33
Q

Describe the structure of phospholipids

A

‘Hydrophillic’ polar phosphate head and ‘hydrophobic’ fatty acid tails

34
Q

Two points

How does triglycerides’s structure related to its function?

A
  • Insoluble in water~does not affect WP or osmosis in cells=storage
  • High ratio of hydrogen:oxygen atoms, release water when oxidised~important source of water
35
Q

How does phospholipids’s structure relate to its function?

A
  • Able to form glycolipids by combining with carbs within cell-surface memberane
  • Polar molecules~fprm a bilayer in aqueous environment=forms a hydrophobic barrier between the inside and outside of a cell
36
Q

What are is the structure of an amino acid?

A

Amino group,carboxyl group,variable group and a carbon bonded to a hydrogen atom

37
Q

How do two amino acids form a dipeptide?

A

The -OH from the carboxyl group and -H from the amino group combine in a condensation reaction to form a dipeptide

38
Q

What are the bonds between amino acids in a polypeptide/protein?

A

Peptide bonds

39
Q

What is the primary structure of a protein?

A

The sequence/order of the amino acids in the polypeptide chain

40
Q

What is the primary structure of a protein determined by?

A

Genetic coding

41
Q
A
42
Q

What is the secondary structure of a protein?

A

How the protein/polypeptide chain is folded e.g α-helix

43
Q

What is the tertiary structure of a protein?

A

The complex 3D shape

44
Q

What are the bonds in the tertiary structure of a protein + description?

A
  • Disulfide~strong,not easily broken
  • Ionic~easily broken by pH change
  • Hydrogen~numerous but broken easily
45
Q

What are fibrous proteins?

A

Proteins with structural functions

46
Q

What are globular proteins?

A

Proteins which carry out metabolic functions

47
Q

Describe the test for proteins

A
  1. Add equal volume of sample and Na(OH)2 solution
  2. Few drops of copper(II) solution
    Purple colouration=protein
    Remains blue=no proteins
48
Q

How do enzymes increase ROR?

A
  1. Provide an alternative pahtway for the reaction with a lower activation energy
  2. By forming an enzyme-substarte complex
49
Q

What is the function of an enzyme determine by?

A

Its tertiary structure

50
Q

Describe the induced-fit model of enzyme action

A

The active site moulds itself around the substrate as the
enzyme-substrate complex is formed
The shape of the active sighlt changes

51
Q

What is a competitive inhibitor?

A

A substance which binds to the active site of an enzyme reducing its activity

52
Q

What is a non-competitive inhibitor?

A

A substance which binds to a different position on a enzyme,which is not the active site. Indirectly reducing its actvity

52
Q

Why can a competitive inhibior bind to an enzyme?

A

The substance has a similar structure to the substrate which binds to the enzyme,allowing it to fit into the active site of the enzyme

53
Q

How can the effect of an inhibior be reduced?

A

Increase the concentration of the substrate

54
Q

What happens when a non-competitive inhibitor binds to an enzyme?

A

It causes a change in the tertiary structure of the enzyme. This leads toa change in the shape of the active site. This means that the shape is no longer complementary to the substrate

Biology Y12 (10 decks)

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