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Biology Module 2 > 2.1.2 Biological Molecules > Flashcards

2.1.2 Biological Molecules Flashcards

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1
Q

What is the general formula for carbohydrates?

A

Cx(H2O)y

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2
Q

What is a monosaccharide?

A

Single unit of sugar/ carb

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3
Q

What is a disaccharide?

A

Two units of sugar/ carb

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4
Q

What is a polysaccharide?

A

2+ units of sugar/ carb

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5
Q

What is the molecular formula for glucose?

A

C6 H12 06

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6
Q

What is a hexose monosaccharide?

A

A single carb unit made of 6 carbons

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7
Q

How are carbons numbered in a hexose/ pentose ring?

A

Clockwise from the Oxygen atom

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8
Q

What’s the difference between an Alpha and Beta glucose?

A

Position of 0H- group on C1; alpha down; beta up

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9
Q

What are 2 properties of glucose?

A
  1. Polar

2. Soluble in water (OH-)

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10
Q

Why does glucose need to be soluble?

A

Dissolve in cytosol of a cell

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11
Q

How is a gylcosidic bond formed?

A

Condensation reaction between two OH- groups of two glucose molecules, producing H2O

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12
Q

How are glycosidic bonds broken?

A

Hydrolysis reaction between two glucose molecules, using H2O and enzymes

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13
Q

Why are glycosidic bonds broken?

A

To release glucose from energy store

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14
Q

What is a pentose monosaccharide?

A

A single unit of sugar/ carb made of 5 carbons

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15
Q

What are two examples of pentose monosaccharides?

A
  1. Ribose (RNA)

2. Deoxyribose (DNA)

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16
Q

What two polysaccharides is Starch made up of?

A
  1. Amylose

2. Amylopectin

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17
Q

What bonds are in Amylose?

A

1-4 Glycosidic bonds between alpha

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18
Q

What bonds are in Amylopectin?

A

1-6 Glycosidic bonds 1:25 subunits and 1-4

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19
Q

Properties of Amylose? (3)

A
  1. Helix
  2. Compact
  3. Less soluble than glucose
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20
Q

Properties of Amylopectin? (2)

A
  1. Branched

2. More soluble than Amylose

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21
Q

Why is it useful that energy storage molecules (e.g starch) are branched? (2)

A
  1. Compact- store more at once

2. Stable- doesn’t react so easily, retain more glucose

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22
Q

What bonds are in Cellulose?

A

1-4 glycosidic bonds between beta glucose, every other beta upside down

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23
Q

What is the structure of Cellulose?

A

Straight chain

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24
Q

Why is Cellulose used for cell walls? (2)

A
  1. Forms microfibrils (H bonding) -> macrofibrils -> fibres

2. Fibres are strong and insoluble

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25
Q

What shape do 1-4 glycosidic bonds make?

A

Straight

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26
Q

What shape do 1-6 glycosidic bonds make?

A

Branched

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27
Q

Lipids are ____molecules made up of ____

A

Macromolecules; monomers

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28
Q

What does a triglyceride contain?

A

One glycerol molecule and 3 fatty acids

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29
Q

How are triglycerides formed?

A

Esterification; OH- from both molecules react and produce 3 molecules of water

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30
Q

What bonds are in triglycerides?

A

Ester

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31
Q

What kind of a reaction is esterification?

A

Condensation

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32
Q

How are triglycerides broken down?

A

Hydrolysis; water is added and enzyme Lipase (bc Trigl. are lipids)

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33
Q

What is a saturated fatty acid chain?

A

No double bonds

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34
Q

What is an unsaturated fatty acid chain?

A

C=C present

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35
Q

What is a monosaturated fatty acid chain?

A

One C=C present

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36
Q

What is a polysaturated fatty acid chain?

A

More than one C=C present

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37
Q

How do C=C affect triglycerides?

A

Make a kink in the chain, less compact, lower melting point

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38
Q

What is a phospholipid?

A

A triglyceride containing a phosphorus group instead of a 3rd fatty acid chain

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39
Q

Is the glycerol molecule still present in a phospholipid?

A

Yes

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40
Q

Which parts of a phospholipid are polar/ hydrophilic?

A

Phosphate group

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41
Q

Which parts of a phospholipid are non- polar/ hydrophobic?

A

Fatty acid tails

42
Q

What are phospholipids useful for due to their hydrophobic/ hydrophilic nature?

A

Surface active agents

43
Q

What are cell membranes made out of?

A

A phospholipid bilayer

44
Q

What group is cholesterol in?

A

Sterols

45
Q

What is cholesterol used for?

A

Stability and fluidity in cell membranes

46
Q

Where is cholesterol in the cell membrane?

A

The hydrophilic OH- lines up with the hydrophilic phosphate heads of the phospholipids, the hydrophobic carbon rings are in between the hydrophobic fatty acid tails of the bilayer

47
Q

What is the structure of Cholesterol?

A

Hydrophobic carbon rings and a hydrophilic OH- group of the first carbon ring

48
Q

What are peptides made up of?

A

Amino acid monomers

49
Q

What is a protein?

A

One or more polypeptides arranged as complex macromolecules

50
Q

What is the structure of an amino acid?

A

Central carbon, amine group, carboxyl group and R- group

51
Q

How do amino acids join?

A

The OH- group in the carboxyl reacts with the amine forming a peptide bond; a molecule of water is released; catalysed by enzyme

52
Q

How are peptide bonds broken?

A

Protease enzyme catalyses hydrolysis reaction; water is used; amine and carboylic acid group reformed

53
Q

What is a polypeptide?

A

Many amino acids joined

54
Q

What is a dipeptide?

A

Two amino acids joined

55
Q

What is the primary structure of proteins?

A

Amino acid sequence (peptide bonds) directed by info in the DNA

56
Q

What is the secondary structure of proteins?

A

Alpha helix or beta pleated sheet is made by hydrogen bonds between amino acids (not R- group)

57
Q

What is the tertiary structure of proteins?

A

Folding into final 3D shape and R- group interactions

58
Q

What R- group interactions take place in the tertiary structure of proteins?

A
  1. Hydrophobic interactions- phobic inside of protein, philic outside (soluble)
  2. Hydrogen bonds
  3. Ionic bonds
  4. Disulfide bridges
59
Q

Which amino acid can form disulfide bridges?

A

Cystine

60
Q

What is the quaternary structure of proteins?

A

Joining of two or more individual proteins (subunits)

61
Q

What elements are present in carbohydrates?

A

C, H, O

62
Q

What elements are present in lipids?

A

C, H, O

63
Q

What elements are present in proteins?

A

C, H, O, N, S

64
Q

What elements are present in nucleic acids?

A

C, H, O, N, P

65
Q

What are the 3 properties of water?

A
  1. Polar
  2. Hydrogen bonding
  3. High Specific latent heat
66
Q

Why is water polar?

A

2 lone pair of electrons repel = delta negative oxygen and delta positive H = trigonal planar

67
Q

Why can water hydrogen bond?

A

Delta negative oxygen attracted to delta positive hydrogens of other water molecules

68
Q

Why does water have a high specific latent heat?

A

Overcome H bonds

69
Q

What are the 5 functions of water?

A
  1. Solvent
  2. Medium for chemical reactions
  3. Transport medium
  4. Coolant
  5. Habitat
70
Q

Why is water a solvent?

A

Polarity

71
Q

Why is water a medium for chemical reactions?

A

Allows chemicals close proximity to react; high specific heat capacity and pH 7

72
Q

Why is water a transport medium?

A

H bonding; capillary action

73
Q

Why is water a coolant?

A

Prevents big temp changes; high specific heat latency

74
Q

Why is water a habitat?

A
  1. Stable
  2. Ice less dense, insulating
  3. Surface tension, insects
75
Q

How do you test for starch? Positive result?

A

Iodine solution

Brown –> Blue- black

76
Q

How do you test for reducing sugars? Positive result? (name 3)

A
  1. Benedict’s solution
  2. Reagent strips
  3. Colorimetry
77
Q

How do you test for non- reducing sugars? Positive result?

A

Boil in HCl -> Benedict’s solution
Clear blue –> Cloudy brick-red precipitate
Green, yellow, red increasing conc.

78
Q

How do you test for lipids? Positive result?

A

Emulsion test

White emulsion layer

79
Q

How do you test for proteins? Positive result?

A

Biuret’s solution

Blue –> Purple

80
Q

Benedict’s solution procedure?

A

Mix sample with it, heat in water bath

81
Q

Reagent strips procedure?

A

Dip stick into sample, remove, wait for results

82
Q

Colorimetry procedure?

A
  1. Calibrate colorimeter using cuvette of distilled water
  2. Use a range of known conc. of glucose to produce calibration curve
  3. Compare unknown sample to curve
83
Q

How does colorimetry test for reducing sugars?

A

Measures absorbance of light through liquid

More conc = less light passes through (% transmission)

84
Q

In colorimetry, what is transmission?

A

The light that passes through the sample

85
Q

What is a biosenser?

A

Device that detects the presence/ conc. of a biological substance in a solution

86
Q

What is the biosenser mechanism?

A

Analyte present -> Change in transducer -> Signal produced

87
Q

How are retention values (Rf) calculated?

A

Distance moved by solute / distance moved by the solvent

88
Q

In thin paper chromatography, what is the solute?

A

Substance that travels on the paper by the solvent

89
Q

In thin paper chromatography, what is the solvent?

A

Liquid that travels up through the paper

90
Q

What are the 3 types of protein?

A
  1. Globular
  2. Conjugated globular
  3. Fibrous
91
Q

Structure/ properties of Globular proteins? (3)

A
  1. Compact, spherical
  2. Tertiary structure- hydrophilic R- groups outside = soluble
  3. Quaternary structure- mult. polypept.
92
Q

Structure/ properties of Fibrous proteins?

A
  1. Long, thin, rope-like
    2 Insoluble- hydrophobic R-groups
  2. Strong
  3. Quatnerary structure- mult. polypept.
93
Q

What is a conjugated protein?

A

Globular protein containing a prosthetic group

94
Q

What is a prosthetic group? Examples?

A

Globular protein containing a non- polypeptide component

e.g. metal ions, vitamins

95
Q

Insulin: type of protein, structure/ properties, function?

A
  • Globular
  • Soluble
  • Hormone
96
Q

Haemoglobin: type of protein, structure/ properties, function?

A
  • Conjugated globular
  • 4 polypeptides: 2 alpha, 2 beta- opposite to each other
  • Haem group in each chain
  • Soluble
  • Carries oxygen (Cu2+)
97
Q

Why are globular proteins soluble?

A

Hydrophilic R- groups on outside

98
Q

Catalase: type of protein, structure/ properties, function?

A
  • Conjugated globular
  • 4 Haem groups
  • Enzyme for hydrogen peroxide
99
Q

Keratin: type of protein, structure/ properties, function?

A
  • Fibrous
  • Cysteine- disulfide bridges = strong, inflexible and insoluble
  • Structural protein, e.g. skin, hair, nails
100
Q

Elastin: type of protein, structure/ properties, function?

A
  • Fibrous
  • Long, flexible
  • Flexibility to structures, e.g. alveoli
101
Q

Collagen: type of protein, structure/ properties, function?

A
  • Fibrous
  • 3 polypeptides wound together like rop = flexible
  • Strong bonds
  • Connective tissue, e.g. skin, tendons, ligaments

Biology Module 2 (6 decks)

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