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Biology sem 1 > 1.3: Biological Molecules > Flashcards

1.3: Biological Molecules Flashcards

1
Q

what Elements are carbohydrates made from?

A

Carbon, Hydrogen and Oxygen

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2
Q

What is the general formula for carbohydrates?

A

Cx(H20)y

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3
Q

what are Polymers?

A

Monomers joined together in a polymerisation reaction

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4
Q

what are monomers of carbohydrates called

A

Monosaccharides

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5
Q

Two Monosaccharides joined together form..

A

Disaccharides

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6
Q

Many Monosaccharides joined together are called…

A

Polysaccharides

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7
Q

Monosaccharides general formula

A

(CH20)n

N could be from 3 - 7

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8
Q

Characteristics of Monosaccharides

A
  • Sweet tasting
  • Highly soluble in water
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9
Q

Glucose (Monosaccharides) formula

A

C6H12O6 (Hexose sugar)

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10
Q

What are isomers?

A

One of two or more compounds that have the same chemical formula but different arrangements of the atoms. Same chemical formula but different ring structures

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11
Q

What are the isomers glucose forms?

A

Alpha glucose
Beta Glucose

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12
Q

What are the 2 main roles of monosaccharides?

A
  • Source of energy during respiration (due to C-H bonds releasing lots of energy when broken)
  • Important building blocks for larger molecules E.G. glucose is used to make starch
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13
Q

What reaction forms disaccharides?

A

Condensation Reactions

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14
Q

What bond and other properties are formed in a condensation reaction?

A
  • Glycosidic bond
  • Water
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15
Q

Rules for drawing condensation reactions

A
  • always circle the groups
  • always show that water is released
  • always circle & label the bond that is formed
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16
Q

What is the opposite reaction to a condensation reaction?

A

Hydrolisis

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17
Q

What are polysaccharides?

A

Polysaccharides are polymers made of many monosaccharides joined together by glycosidic bonds (condensation reactions)

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18
Q

Properties of polysaccharides

A
  • Not sugar/sweet tasting
  • soluble in water
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19
Q

Starch
- where is it found?
- what are the monomers?

A
  • plants ONLY
  • Alpha glucose
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20
Q

Glycogen
- where is it found?
- what are the monomers?

A
  • Animals & fungi
  • alpha glucose
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21
Q

Cellulose
- where is it found?
- what are the monomers?

A
  • Plants ONLY
  • Beta Glucose
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22
Q

why do organisms use polysaccharides as an energy store instead of glucose?

A
  • glucose is soluble in water
  • accumulation of glucose in the cell would lower the water potential of the cell
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23
Q

What is the main role of starch?

A

Energy store - stored as granules in chloroplasts, seeds and storage organs (e.g. potatoes)

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24
Q

what is starch made up of? (with percentages)

A

Amylose (20%)
Amylopectin (80%)

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25
Q

Amylose
-number of alpha - glucose units per molecule
- branched vs unbranched
- type of glycosidic bond
- colour with iodine solution

A

1) 200-5000
2) unbranched
3) 1,4
4) Deep blue

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26
Q

What is the purpose of turns in the amylose structure?

A

6 glucose turns per unit, which allows molecules to be compact (therefore it takes up less space)

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27
Q

Amylopectin
-number of alpha - glucose units per molecule
- branched vs unbranched
- type of glycosidic bond
- colour with iodine solution

A

1) 5000 -100000
2) branched
3) 1,4 bonds along chain
1,6 between branches
4) stains red/purple

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28
Q

What is the main role of glycogen?

A

Energy store, stores as granules in the muscle and liver.
(branched structure with 1,4 bonds between monomers and 1,6 between branches)
shorter chains and more branches

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29
Q

What is the role of cellulose in plants?

A

To provide structural support

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30
Q

What is Cellulose made of?

A

Beta- glucose monomers joined by glycosidic bonds.

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31
Q

What is the difference in OH groups on carbon 1 between alpha and beta glucose?

A

Alpha glucose - OH is below
Beta glucose - OH is above

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32
Q

cellulose structure

A
  • Monomers need to be rotated 180 degrees to be joined to next one
  • Forms straight unbranched chains, they run parallel
  • cross linked parallel chains using hydrogen bonds
  • weak but together bonds cause the cellulose to be extremely strong
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33
Q

What are microfibrils?

A

60-70 tightly cross-linked cellulose molecules

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34
Q

How are microfibrils linked together?

A

Using hydrogen bonds which form cellulose fibrils

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35
Q

Where is cellulose found?

A

In the plants cell wall, makes upto 20-40% of the plant cell wall

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36
Q

cellulose functions for cell wall

A
  • cellulose fibres run in different directions which provides rigidity
  • Cell wall is fully permeable and it has high tensile strength, which prevents cell from bursting when water enters by osmosis
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37
Q

What are proteins made of?

A

Monomers called amino acids which make up more than 50% of the dry mass cells

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38
Q

What are the functions of protein?

A
  • cell membrane components
  • enzymes which control cellular reactions
  • haemoglobin (o2 transport)
  • keratin, protein which strengthens hair and nails
  • immune response
  • collagen, protein, strengthens bones and arteries
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39
Q

How many types of amino acids are there?
Essential / non-essential

A

20 types of amino acids
8 essential (must be present in diet)
12 non-essential, can make on own
same general structure

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40
Q

How do amino acids vary?

A

chemical elements found in the R group

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41
Q

How are dipeptides formed? What is the bond formed?

A

Two amino acids joined together by condensation reaction.
Peptide bond is formed

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42
Q

What is protein folding?

A

Where polypeptide chains are folded in a series of stages so that they can carry out specific functions and have a correct 3D shape

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43
Q

How are polypeptides formed?

A

Amino acids linked together by peptide bonds

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44
Q

How many polypeptide chains form collagen?

A

3

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45
Q

What is the primary structure in protein folding?

A

The order and sequence of the amino acids in the polypeptides chain.
Ultimately responsible for the final shape due to changing the amino acids in the sequence can change the function

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46
Q

Protein folding - secondary structure
What does it mean?

A

When the polypeptide chain starts to fold to become more compact.

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47
Q

What shape does a polypeptide chain form?

A

An alpha helix or a beta pleated sheet. Held together by hydrogen bonds.

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48
Q

Alpha Helix structure (protein folding)

A

Hydrogen bonds form between amino acids 4 residues apart.
Form part of the carboxylic group of one amino acid and part of the amine group another 4 spaces away

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49
Q

Beta Pleated sheet structure (protein folding)

A

Folded into a flat structure with amino acid chains running alongside each other and held together by hydrogen bonds

50
Q

What is the tertiary structure (protein folding)

A

How the secondary structure present in the polypeptide chain fold together to produce a precise 3D shape

51
Q

How is the tertiary structure shape held together (4 bonds)

A
  • Hydrogen bonds
  • Ionic bonds
  • Disulphide bonds
  • Hydrophobic bonds
52
Q

How can hydrogen bonds form in amino acids?

A
  • Can occur between polar R groups of different amino acids
  • Forms between part of the carboxylic group of one AA and part of the anime group of another
53
Q

How can hydrogen bonds be broken?

A

By high temperature or PH changes

54
Q

When do ionic bonds occur?

A

Between oppositely charged R groups of different AA

55
Q

How are ionic bonds broken?

A

By PH changes

56
Q

What are R groups (amino acids)

A

another atom or group of atoms bonded to the central atom

57
Q

When do Disulphide bonds occur?

A

Between R groups of different cysteine AA

58
Q

How are disulphide bonds broken?

A

By reducing agents

59
Q

How do hydrophobic interactions occur?

A

Between non polar of hydrophobic R groups of different amino acids so that they try to come close together away from water

60
Q

What is the quaternary Structure? (polypeptide bonds)

A

Is the association of two or more polypeptide chains. The associated chains are held together by 4 types of bonds. (hydrogen, ionic. disulphide, hydrophobic.)

61
Q

What does hydrophobic mean?

A

doesn’t like water, this means they will concentrate themselves into the centre of the protein

62
Q

What does hydrophilic mean?

A

Likes water, so will more likely be on the outside of the protein

63
Q

What is an example of a reducing sugar?

A

Glucose

64
Q

What reagent is used to test for reducing sugar?

A

Benedict’s reagent

65
Q

What is the method used to test for reducing sugars?

A
  • Add a few drops of Benedict’s reagent
  • Put the test tube in a water bath and heat 80-90c for 10 minutes
66
Q

What is a positive result of the reducing sugars test?

A

Brick red/orange

67
Q

What is a negative result of the reducing sugars test?

A

Blue

68
Q

What solution is used to test for starch?

A

iodine solution

69
Q

What is the method for testing for starch?

A
  • Add 5cm cubed of iodine solution to the substance
  • watch to see whether the result is positive or negative
70
Q

What is the positive result for starch?

A

blue/black colour

71
Q

What is a negative result for starch?

A

Brown/orange

72
Q

What reagent is used for non-reducing sugars?

A

Benedict’s reagent

73
Q

What is an example of a non-reducing sugar?

A

Sucrose

74
Q

What is the method to test for non-reducing sugars?

A
  • Test for reducing sugars originally, if the test obtains a negative result then get a fresh sample.
  • using the fresh sample add hydrochloric acid to break the glycosidic bonds.
  • Then neutralise the sample with sodium hydrogen carbonate solution
  • Add the Benedict’s reagent to the sample and place into a water bath, heating @ 90 degrees for 10 minutes
75
Q

What is a positive result for non-reducing sugars?

A

brick red/orange

75
Q

what is the negative result for non-reducing sugars?

A

Blue

76
Q

What reagent is used to test for proteins?

A

Buiret reagent

76
Q

What must you NOT do with the method of the protein food test?

A

Heat the buret reagent

77
Q

What is the method used to test for proteins?

A

Add biuret reagent containing sodium hydroxide and copper sulphate to the sample

77
Q

What is a positive result of the proteins test?

A

Lilac/purple colour

78
Q

What is a negative result of the proteins test?

A

Blue colour

79
Q

What is the emulsion test for?

A

Lipids

80
Q

What is used to test for lipids?

A

Absolute Ethanol

81
Q

What is the method used for the lipids test?

A

Add absolute ethanol to the sample and then shake. Pour the top part of the liquid into water and shake again. You should then see a positive or negative result

82
Q

What is a positive result of lipids?

A

A white cloudy emulsion/ milky white emulsion

83
Q

What is a negative result of lipids?

A

It would be colourless or transparent

84
Q

What is an example of a globular protein with a quaternary structure?

A

Haemoglobin

85
Q

What is a haemoglobin molecule made of?

A

Four polypeptide chains - two alpha chains and two beta chains held together by hydrogen bonds. Contains a haem group also

86
Q

What is a haem group and what is it usually called?

A

a group containing a Fe2+ ion (iron)
called a prosthetic group as its part of a protein made from amino acids.

87
Q

What can one molecule of oxygen do with the haem group?

A

Bind reversibly with the iron in the haem group

88
Q

How much can each molecule of haemoglobin carry?

A

4 molecules of oxygen (O2)

89
Q

In haemoglobin folding what do the hydrophilic r groups do in the amino acids?

A

arrange themselves outside of the haemoglobin molecule, making it soluble

90
Q

In haemoglobin folding what do the hydrophobic r groups do in the amino acids?

A

arrange themselves on the inside of the haemoglobin molecule which helps to maintain the shape of the molecule

91
Q

Is haemoglobin unstable or stable?

A

unstable, not fully rigid due to needing flexibility

92
Q

What is an example of a fibrous protein in a quaternary structure?

A

Collagen

93
Q

What is each collagen molecule made of?

A

3 helical polypeptide chains arranged in a triple helix held together by hydrogen bonds.

94
Q

Why is the collagen molecule closely packed?

A

because every 3rd amino acid in the polypeptide chain is glycine which is the smallest amino acid (just contains hydrogen)

95
Q

Where is collagen found?

A

Tendons, skin and connective tissue

96
Q

What bonds can collagen molecules form with each other?

A

covalent bonds with parallel collagen molecules

97
Q

What do the covalent bonds form?

A

collagen fibrils

98
Q

What do the covalent bonds cross links do?

A

They are staggered which increases tensile strength of the fibril

99
Q

What are lipids?

A

Lipids are a diverse group of chemicals.

100
Q

What are the most common types of lipids?

A

triglycerides - found in fats and oils

101
Q

What is triglycerides made from?

A

1 glycerol molecule and 3 fatty acids joined together in a condensation reaction and linked by ester bonds

102
Q

What are ester bonds?

A

forms when a hydroxyl (-OH) group from the glycerol bonds with the carboxyl (-COOH) group of the fatty acid

103
Q

What are the features of the hydrocarbon fatty acid tail?

A
  • hydrophobic
  • Insoluble in water
104
Q

What is the difference between saturated and unsaturated fatty acid?

A

saturated: have hydrocarbon chains connected by single bonds only.

unsaturated: have one or more double bonds

105
Q

What does the bond between neighbouring carbon atoms do to the structure?

A

Leads to a kink in the hydrocarbon chain

Increases the fluidity of the lipid formed (oils have more C=C that fats

As it reduces the intramolecular forces so fatty acids cant pack as closely together

106
Q

what is the difference between monounsaturated and polyunsaturated fatty acid?

A

Monounsaturated: one c=c double bond in the hydrocarbon chain

polyunsaturated: more than one c=c double bond in the hydrocarbon chain

107
Q

What are the roles of triglycerides?

A
  • source of energy for the body
  • used to make water / metabolise water
  • insulator
  • bouyancy
108
Q

What are phospholipids?

A

a special type of lipid found in a cell membranes.

109
Q

What is the difference between lipids and phospholipids?

A

One of the fatty acid tails is replaced by a phosphate group.

110
Q

What are the features of the phospholipid structure?

A

head of the phospholipid is hydrophilic (water loving) and the tail is hydrophobic (water hating).

111
Q

What are the roles of phospholipids?

A
  • major components of cell membranes as they form a bilayer when in water
  • responsible for the partially permeable nature of cell membranes and allow lipid soluble substances to enter and leave the cell and prevent water soluble substances from entering and leaving the cell.
112
Q

What are the 3 regions of cholesterol?

A
  • hydrocarbon tail
  • ring structure
  • hydroxyl group
113
Q

What is the hydroxyl group in cholesterol characteristics?

A

polar which makes this part of the molecule soluble in water (hydrophilic)

114
Q

What is the ring structure and hydrocarbon chain in cholesterol characteristics?

A

This part is non-polar and makes this part of the molecule insoluble in water (hydrophobic) but it is fat soluble.

115
Q

What is the definition of a fat soluble and water soluble region in the same molecule?

A

Amphipathic molecule

116
Q

What is the role of cholesterol?

A
  • regulates membrane fluidity in cell membranes
  • makes membranes less fluid at high temps and more fluid at low temps
  • reduce side to side movement of phospholipids.
  • increases the mechanism stability of the cell
  • prevents leakage of water and dissolved ions from the cell.
117
Q

Are fatty acids alkali or acid?

A

acid, so lowers the PH

Biology sem 1 (9 decks)

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