Aspects of Biochemistry Flashcards

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1
Q

What is biochemistry?

A

Biochemistry is the study of biological molecules and their roles in living organisms

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2
Q

List the biological molecules.

A

Water, Carbohydrates, Nucleic Acids, Lipids , Proteins

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3
Q

What is Metabolism?

A

Chemical rection that occurs in organisms

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4
Q

What is Anabolism?

A

The building up larger biological molecules from smaller ones.

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5
Q

What is Catabolism?

A

The breaking down large biological molecules into smaller ones

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6
Q

What are the elements that make up carbohydrates?

A

Carbon (C),Hydrogen(H) and Oxygen(O)

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7
Q

What are the elements that make up water?

A

Hydrogen (H) and Oxygen (O)

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8
Q

What are the elements that make up Nucleic Acids?

A

Nitrogen(N), Phosphorus(P), Carbon (C),Hydrogen(H) and Oxygen(O).

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9
Q

What are the elements that make up Protein?

A

Nitrogen(N), Sulphur(S), Carbon (C),Hydrogen(H) and Oxygen(O).

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10
Q

What are the elements that make up Lipids?

A

Carbon (C),Hydrogen(H) and Oxygen(O).

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11
Q

What polymer does alpha-glucose form when chemically bonded together?

A

maltose

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12
Q

what polymer does beta-glucose form when chemically bonded together?

A

cellulose

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13
Q

how are glycosidic bonds formed?

A

formed via condensation reaction between two monosaccharides.

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14
Q

how do you remove/break glycosidic bonds?

A

hydrolysis reaction( adding water)

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15
Q

What are some characteristics of disaccharides?

A

Soluble and taste sweet.

Function as a transport form

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16
Q

What is a reducing sugar?

A

A reducing sugar is a sugar that in solution has an aldehyde or a ketone group.

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17
Q

Give 2 examples of reducing sugars.

A

glucose and fructose.

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18
Q

What is sucrose? what are characteristics of sucrose?

A

sucrose, also know as table sugar, is the main form in which carbohydrates are transported in plants.

Formed by plants for transport in phloem.

Important source of energy in humans.

Sucrose is polar and water soluble.

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19
Q

What is starch a mixture of?

A

Contains a mixture of amylose and amylopectin

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20
Q

Characteristic of starch.

A

Insoluble; easily broken down my the enzyme amylase.

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21
Q

Characteristics of amylose.

A
  1. straight chain
  2. made from alpha glucose molecules
  3. has alpha 1-4 glycosidic linkage.
  4. Turns to dark blue/black colour in starch test.
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22
Q

Characteristics of amylopectin.

A
  1. branched
  2. made from alpha glucose molecules
  3. has alpha 1-4 and 1-6 (causes branching) glycosidic linkages
  4. Turns reddish brown colour in starch test.
  5. Cannot be hydrolysed by the enzyme amylase because of the glycosidic linkages
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23
Q

List some similarities between amylose and amylopectin.

A
  1. Both are polysaccharide molecules.
  2. Both are made of α-glucose units/molecules.
  3. Both have α 1-4 glycosidic linkages.
  4. Both types are found in starch granules.
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24
Q

Characteristics of glycogen

A
Extremely branched ( more than
amylopectin)

Made up of α-glucose molecules;
α1,4 and α1,6 glycosidic
linkages.

Functions as energy storage in
animals, fungi and some bacteria.

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25
Q

Characteristics of cellulose

A

Made up of β-glucose

Linked with β1-4 glycosidic bonds.

Cellulose molecules do not coil, but lie straight (unbranched).

Hydrogen bonds prevents twisting in the molecule.

Good source of fibre

Multiple cellulose molecules form microfibrils which are responsible for
providing strength in plant cell walls.

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26
Q

What are the forms of startch?

A

Amylose and amylopectin

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27
Q

How is a unbranched chain formed?

A

(A 1,4 glycosidic bond). Formed between C1 at the end of a growing chain and the C4 of a glucose monomer.

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28
Q

How is a branched chain formed?

A

(A 1,6 glycosidic bond) .Formed by adding a glucose monomer to C6 on a growing chain.

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29
Q

Name 3 energy storage polysaccharides

A

Amylose, Amylopectin and Glycogen

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30
Q

What are the basic units of lipids?

A

fatty acids

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31
Q

What are the classifications of fats?

A

saturated and unsaturated

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32
Q

What are saturated fats?

A

Contains carbon to carbon single bonds, and is solid at room temperature

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33
Q

What is a triglyceride?

A

A lipid made up of three fatty acids attached to a glycerol

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34
Q

What ends a fatty acid chain?

A

A carboxyl group

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35
Q

How are ester bonds formed?

A

When the carboxyl group on the fatty acid molecule binds with the hydroxyl group on the glycerol .

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36
Q

Characteristics of triglycerides?

A

Insoluble in water (hydrophobic)
Triglycerides are rich in energy and make excellent long term energy
storage molecules.
More efficient for energy storage than carbohydrates

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37
Q

Where are triglycerides stored?

A

Adipose tissue in animals and in oil droplets in plants

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38
Q

What is a phospholipid?

A

A lipid made up of one glycerol, two fatty acids and a phosphate group attached to the glycerol.

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39
Q

What happens when food is scare?

A

When food is scare, people are in negative energy balance and require more energy than they can obtain in their diet

40
Q

What happens when food isn’t scare?

A

People are in a positive energy balance and store excess energy as fat, and may become overweight or obeseq.

41
Q

What happens when food isn’t scare?

A

People are in a positive energy balance and store excess energy as fat, and may become overweight or obese.

42
Q

What are the building blocks(monomers) of protein?

A

Amino acidsq

43
Q

What are proteins?

A

Substances/macromolecules made up of many long chain amino acids know as polypeptides.

44
Q

What are amino acids composed of?

A

A central carbon which forms bonds with an amine group, a carboxyl group, a hydrogen atom and a residual group (any other group).

45
Q

When are amino acids linked together?

A

During protein synthesis by a condensation reaction.

46
Q

How are peptide bonds formed?

A

When amino acids are linked together during protein synthesis by a condensation reaction.

47
Q

Where does the peptide bond form in the amino acids?

A

Between the carboxyl group (-COOH) of one amino acid and the amine group (-NH2) of the other.

48
Q

What is a polypeptide?

A

A long chain of amino acids

49
Q

What breaks a peptide bond?

A

Hydrolysis reaction

50
Q

Property of cysteine

A

adjacent Cysteines can bond together to form disulphide bonds ( because of their SH R group)

51
Q

What determines the sequence of amino acids?

A

Genes

52
Q

What is a peptide?

A

Short chain of amino acids

53
Q

What is a dipeptide?

A

Compound formed when 2 amino acids are linked together.

54
Q

What is a tripeptide?

A

Compound formed when 3 amino acids are linked together

55
Q

Draw the peptide bond.

A

H - N - C = O

56
Q

What is the primary structure of protein organization?

A

This is the sequence of amino acids linked together in a polypeptide/protein.
It is determined by a gene.

57
Q

What does the sequence of amino acids determine?

A

The structure and function of a protein

58
Q

What is a gene?

A

A gene is a length of DNA which carries a code that determines the sequence in which amino acids are linked together on a ribosome to form a polypeptide.

59
Q

What is the secondary structure of protein organization?

A

The sequence of amino acids fold in different ways.

They may coil into an α-helix or they may adopt a sheet like pattern called a β- pleated sheet.

60
Q

What maintains the secondary structure of the protein?

A

Each pattern is maintained by hydrogen bonds that form between different amino acids

61
Q

Give an example of a secondary structure protein made up of alpha helices.

A

Keratin

62
Q

Where are hydrogen bonds formed in alpha helix?

A

Hydrogen bonds form between the oxygen of the carboxylic group (-COO)of one amino acid and the hydrogen to the amine group (NH2) of another amino acid four places ahead of its chain
So, amino acid 1 and 5 are bonded

63
Q

Where are hydrogen bonds formed in beta pleated sheet?

A

Hydrogen bonds are formed between the C=O and NH groups of one chain and the
NH and C=O groups of adjacent chains.

64
Q

Give an example of a secondary structure, made up of beat pleated sheet.

A

Silk, which is made of the protein fibroin

65
Q

What is the tertiary structure of protein organization?

A

In this structure the polypeptide chain is able to fold on itself even more into a 3d shape.
The tertiary structure is held together by hydrogen bonds and interaction between R groups (disulphide bonds, Van Der Waals Forces and Ionic interactions ).

66
Q

Give an example of a tertiary structure, made up of beat pleated chains.

A

Haemoglobin molecule.

67
Q

Explain the tertiary structure of the haemoglobin molecule.

A

Each of the polypeptide chains winds itself around a little group of atoms with an iron ion (Fe2+) at the centre. This group is called a haem group.

68
Q

Why is a haem group considered a prosthetic group?

A

Because it makes up part of the protein but it is not an amino acid.

69
Q

What is the quaternary structure of protein organization?

A

This is a highly complex protein structure consisting or more than one polypeptide chain.

70
Q

What is haemoglobin?

A

It is the red oxygen-carrying pigment found in red blood cells.

71
Q

List four bonds that stabilize proteins.

A

hydrogen bonds form between polar groups,
ionic bonds form between ionised amine and carboxylic acid groups
hydrophobic interactions between non-polar side chains
disulphide bonds between the S-containing R groups of cysteines.

72
Q

What forms fibers?

A

Fibrils

73
Q

What forms fibrils?

A

Collagen molecules link together to form fibrils (Collagen has tremendous tensile strength as a result of these fibres)

74
Q

Give examples of globular proteins.

A

Haemoglobin, enzymes, antibodies, some hormones like insulin

75
Q

Give examples of fibrous proteins.

A

Collagen, Keratin, Elastin.

76
Q

How many polypeptide chains make up haemoglobin?

A

4 separate polypeptide chains of 2 different types ( 2 alpha and 2 beta)

77
Q

How many amino acids does an alpha chain have in haemoglobin?

A

141 amino acids

78
Q

How many amino acids does a beta chain have in haemoglobin?

A

146 amino acids

79
Q

Properties of Globular protein.

A
  1. Soluble in water
  2. Folded into a complex 3d shape/structure
  3. Metabolically active
80
Q

Properties of Fibrous protein.

A
  1. Insoluble in water
  2. Folded into a simple shape (e.g helix)
  3. Metabolically unreactive
81
Q

What is obesity?

A

Obesity is a medical condition in which the body stores large amounts of excess fat; this leads to health risks.

82
Q

What is obesity?

A

Obesity is a medical condition in which the body stores large amounts of excess fat; this leads to health risks.

83
Q

What is used to test for starch?

A

Iodine

84
Q

What is the colour change in a starch test?

A

Yellow/Orange to Blue-black/Blue

85
Q

What is used to test for reducing sugars?

A

Benedict’s Solution

86
Q

What is the colour change in a reducing sugar test?

A

blue to green to yellow to orange to red with a precipitate

87
Q

What is used to test for non- reducing sugars?

A

dilute hydrochloric acid, sodium hydrogen carbonate and Benedict’s solution.

88
Q

What are some functions of protein?

A
89
Q

What is used to test for proteins?

A

Biuret solution

90
Q

What is used to test for lipids?

A

Ethanol

91
Q

What is the colour change in a protein test?

A

Blue to violet to purple to lilac

92
Q

What shows a positive lipid test?

A

white cloudiness an emulsion (White cloudiness)

93
Q

Why are triglycerides better for energy storage than starch?

A

Triglyceride molecule is hydrophobic and so it is closely packed together ( it doesn’t have a OH) group, so it is well situated for energy content than carbohydrates

94
Q

Name the primary storage polysaccharide of plants

A

Starch

95
Q

Name two plant organs in which it accumulates.

A

seeds, stems, roots or tubers

96
Q

Why is starch stored in plants instead of glucose?

A

plants store food in form of starch instead of glucose since glucose is soluble in water it is harder to store because it increases the concentration of the cells but starch is an insoluble molecule, therefore, it can be stored in the cells.