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Biology Year 1 > Chapter 1 - Biological Molecules > Flashcards

Chapter 1 - Biological Molecules Flashcards

1
Q

What are polymers

A

Long molecules made up of many smaller molecules

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2
Q

What are monomers

A

Small molecules that make up polymers

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3
Q

What is the polymer of carbohydrates

A

Polysaccharide

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4
Q

What is the monomer of carbohydrates

A

Monosaccharides (eg glucose)

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5
Q

What is the polymer of proteins

A

Polypeptide chain/protein

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6
Q

What is the monomer of a protein

A

Amino acids

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7
Q

What is the monomer of fats/lipids

A

Triglycerides

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8
Q

What is the polymer of nucleic acids

A

DNA/RNA

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9
Q

What is the monomer of nucleic acids

A

Nucleotides

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10
Q

What is a condensation reaction

A

When 2 molecules join together to form one larger molecule and one molecule of water

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11
Q

What is a glycosidic bond

A

A bond between molecules in carbohydrates

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12
Q

How is a glycosidic bond formed

A

Through a condensation reaction

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13
Q

What is a hydrolysis reaction

A

When molecules are split apart using a molecule of water

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14
Q

?

A

?

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15
Q

What is a disaccharide

A

A molecule made up of 2 monosaccharides

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16
Q

What is the disaccharide maltose made up of

A

Glucose + Glucose

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17
Q

What is the disaccharide sucrose made up of

A

Glucose + Fructose

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18
Q

What is the disaccharide lactose made up of

A

Glucose + Galactose

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19
Q

What is the formula for glucose

A

C6H12O6

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20
Q

What are the 2 forms of glucose

A

Alpha

Beta

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21
Q

What does alpha glucose look like

A

H at the top

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22
Q

What does beta glucose look like

A

H at the bottom

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23
Q

What is a polysaccharide

A

Many monosaccharides joined together

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24
Q

What reaction occurs to join monosaccharides together to form polysaccharide

A

Condensation reactions

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25
Q

What are 3 examples of polymers of carbohydrates

A

Cellulose
Starch
Glycogen

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26
Q

Where is cellulose found

A

Plant cell walls

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27
Q

What is cellulose made from

A

Beta glucose

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28
Q

What bonds are found in cellulose

A

Glycosidic Bonds

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29
Q

How can the structure of cellulose be described

A
  • Unbranched/straight chain
  • Has more strength (to hold cells and protect)
  • Insoluble (no effect on water potential so no effect on osmosis)
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30
Q

What are the 2 types of starch

A

Amylose

Amylopectin

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31
Q

Where are both amylose and amylopectin found

A

In plants, for energy storage (glucose), and for respiration

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32
Q

What are both types of starch made from

A

Alpha glucose

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33
Q

What bonds are found in both amylose and amylopectin

A

Glycosidic bonds

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34
Q

What are amylose and amylopectin

A

Types of polymers of starch

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35
Q

How can the structure of amylose be described

A
  • Unbranched and coiled (to compact storage of glucose)

- Insoluble (doesn’t effect water potential so no effect in osmosis)

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36
Q

What is cellulose made from

A

Beta glucose

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37
Q

What bonds are found in cellulose

A

Glycosidic Bonds

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38
Q

Where are both amylose and amylopectin found

A

In plants, for energy storage (glucose), and for respiration

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39
Q

How can the structure of amylopectin be described

A
  • Branched (increase surface area, so can be hydrolysed more quickly)
  • Insoluble, so no effect on water potential and no osmosis
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40
Q

Where is glycogen found

A

In animals, for glucose/energy storage

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41
Q

What is glycogen made from

A

Alpha glucose

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42
Q

What bonds are found in glycogen

A

Glycosidic bonds

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43
Q

How can the structure of glycogen be described

A
  • Branched (more than amylopectin) so Increase surface area for faster hydrolysis
  • Insoluble so no effect on water potential or osmosis
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44
Q

What is the test for starch

A

1) Add iodine to sample

2) Turns blue/black if present, stays orange if negative

45
Q

What is the test for carbohydrates

A

Benedicts test

46
Q

What can the benedicts test be used for

A

Carbohydrates, both reducing sugars and non-reducing sugars

47
Q

What is the benedicts test for reducing sugars

A

1) Add benedicts solution
2) Heat in water bath to 100c
3) Turns red if present, blue if not

48
Q

What do you do if benedicts test for reducing sugars remains blue

A

Test for non reducing sugars
1) Add hydrochloric acid
2) Heat in water bath to 100c
3) repeat test for reducing sugar
4) If red, non-reducing sugar is present
If blue, there are no carbs/sugar present

49
Q

What is the monomer of lipids/fats

A

Triglycerides

50
Q

What are triglycerides made up of

A

Glycerol and fatty acids

51
Q

Draw glycerol next with 3 fatty acids

A

3.1.3

52
Q

Draw a triglyceride

A

Glycerol and 3 fatty acids joined

3 water molecules off of it

53
Q

What are the characteristics of a saturated fatty acid

A

Don’t have double bonds between carbon atoms

54
Q

What do saturated fatty acids cause

A

An increases in cholesterol and low density lipoproteins

55
Q

What are the characteristics of unsaturated fatty acids

A

Have double bonds between carbon atoms, causing a kink in its chain

56
Q

What do unsaturated fatty acids have less of

A

Hydrogen atoms, because of their double bonds between carbons

57
Q

What 3 elements do lipids contain

A

Carbon
Hydrogen
Oxygen

58
Q

What bonds are in lipids

A

Water bonds

59
Q

What does saturated/unsaturated triglyceride refers to

A

The fatty acids on it, whether they have double bonds between carbons or not

60
Q

What is the function of a triglyceride

A

Store of energy

61
Q

How can the structure of triglycerides be explained

A
  • Long polymers with many bonds

- Insoluble, so no effect on wp or osmosis

62
Q

What do triglycerides form inside cells

A

Fat droplets

63
Q

Draw and label a fat droplet

A

Looks like jelly fish in a circle

Hydrophilic heads point outwards

64
Q

Draw a phospholipid

A

Glycerol in middle
Phosphate group (hydrophilic head) in left
2 fatty acids, bonded by water bonds, on the right

65
Q

What is the function of phospholipids

A
  • Form cell membranes

- Control what goes in and out of a cell

66
Q

What is a phospholipid bilayer

A

When a cell membrane consists of 2 layers of phospholipids, tails are always pointing inwards

67
Q

Why are the tails of phospholipids always pointing inwards in a phospholipid bilayer

A

To make the middle hydrophobic so that it is difficult for polar molecules eg water to diffuser through

68
Q

What is the test for lipids called

A

The emulsion test

69
Q

What is the emulsion test

A

1) Mix substance with ethanol
2) Add water
3) If positive there will be a cloudy white layer

70
Q

What is a protein

A

A polymer of amino acids

71
Q

What is essential to a proteins function

A

It’s shape

72
Q

What are amino acids

A

The monomers that make up proteins

73
Q

Draw an amino acid

A

On left: N with 2 H’s
Middle : R group at top, C, H
On right: COOH, C bonded to O and OH

74
Q

What is a dipeptide

A

2 amino acids that are joined by a peptide bond

75
Q

How do a dipeptide form

A

2 amino acids bonds through a condensation reaction (water molecule released)

76
Q

Draw a dipeptide being formed

A

C double bonds to O

Bonded to N which is bonded to H

77
Q

How to remember the types of proteins

A

EATS

78
Q

What does EATS stand for (proteins)

A

Enzymes
Antibodies
Transport
Structural

79
Q

What is the test for proteins

A

Biuret test

80
Q

What is the biuret test

A

1) Add biuret reagent/solution (blue)
2) If present, will be purple/lilac
If not, stays blue

81
Q

How do you describe a primary structure protein

A

A sequence of amino acids

82
Q

What bonds are in a primary structure protein

A

Peptide

83
Q

How do you describe a secondary structure protein

A

Long chains of amino acids that fold into regions with repeating patterns

84
Q

What bonds are in a secondary structure protein

A

Peptide

Hydrogen

85
Q

How do you describe a tertiary structure protein

A

The final 3D testing shape of the protein

86
Q

What bonds are in a tertiary structure protein

A
  • Peptide bonds
  • Hydrogen bonds
  • Ionic bonds
  • Disulphide bridges
87
Q

What do disulphide bridges do

A

Connect 2 different regions

88
Q

How do you describe a quaternary structure protein

A

Proteins made up from more than one polypeptide chain

89
Q

Example of a protein with a quaternary structure

A

Haemoglobin

90
Q

What bonds are in a quaternary structure protein

A
  • Peptide
  • Hydrogen
  • Ionic
  • Disulphide
91
Q

How to structure an answer to a question about the shape of a protein and how it performs its function

A
  • Tertiary structure of protein
  • Means active site is
  • Complementary in shape to substrate
  • So enzyme-substrate complex forms
92
Q

What are 2 ways that a protein may be non-functional

A

Mutation

Denatured

93
Q

How does a mutation or denaturing cause a protein to be non-functional

A
  • Changes tertiary structure
  • Changes shape of active site
  • Substrate is not complementary
  • Enzyme-substrate complex can’t form
94
Q

What is meant by denaturing

A

A permanent change to the shape of the active site of a protein
Meaning enzyme-substrate complex’s can’t form

95
Q

What is an enzyme catalyse reaction

A

A reaction that’s activation energy falls as it is catalysed

96
Q

What are 5 factors affecting the rate of enzyme catalysed

A
  • temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
  • Inhibitions (competitive and non-competitive)
97
Q

How does an increase in temperature (to optimum) effect reactions

A
  • Increase collisions
  • Higher % of collisions have activation energy
  • More enzyme-substrate complexes can form
98
Q

How does an increase in temperature after its optimum effect reactions

A
  • Bonds break as molecules vibrate
  • Active site shape changes
  • Can’t form enzyme-substrate complex’s
99
Q

What effect does an increase or decrease from the optimum pH of the reaction have

A

Causes enzyme activity (rate of reaction) to fall

100
Q

Why does the rate of reaction fall if the pH is not at its optimum

A
  • Hydroxyl (alkaline) or hydrogen (acidic) ions will interact with hydrogen or Ionic bonds
  • Changes shape of tertiary structure
  • Change shape of active site
  • fewer enzyme-substrate complex’s
  • Enzyme denatured
101
Q

How does enzyme concentration effect the rate of reaction

A
  • Increase causes increase (positive correlation)

- More possibility for enzyme-substrate complex’s to form

102
Q

How may an increase in enzyme concentration not increase the rate of reaction

A
  • Substrates May be running out

- Therefore they will be the limiting factor

103
Q

How does substrate concentration effect the rate of reaction

A
  • Increase as it increases
  • More possible collisions
  • More enzyme-substrate complex’s
104
Q

How may an increase in substrate concentration cause no change in rate of reaction

A
  • All active sites may become occupied

- Enzyme concentration becomes limiting factor

105
Q

What do competitive inhibitors do

A

Bind to active site of enzyme, so enzyme-substrate complex’s can’t be formed

106
Q

What will an increase in competitive inhibitors do to effect the rate of reaction

A
  • Bing to active sites of proteins

- Deny Enzyme-Substrate complex’s

107
Q

What do non-competitive inhibitors do

A
  • Bind to Enzyme not at the active site

- Distort shape of active site

108
Q

How will an increase in non-competitive inhibitors effect the rate of reaction

A
  • Decrease opportunity for enzyme-substrate complex’s

Biology Year 1 (10 decks)

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