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Biology > Chapter 1: Biological molecules > Flashcards

Chapter 1: Biological molecules Flashcards

1
Q

What is Molecular Biology?

A

The study of particular groups of biological molecules found in living organisms.

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2
Q

What is Covalent Bonding?

A

A bond between atoms share a pair of electrons in their outer shells. Forms a more stable molecule.

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3
Q

What is Ionic Bonding?

A

A bond formed between ions of opposite charge attracting one another. They are weaker than covalent bonds. (eg. Na+ and Cl- making sodium Chloride)

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4
Q

What is Hydrogen Bonding?

A

The attraction of the negative charges region of a polarised molecule to the positively charged region of another, forming a weak electrostatic bond. (Individually Weak, Collectively Strong)

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5
Q

Whats is a polar molecule?

A

A molecule with unevenly distributed charge of electrons, this causes separate positively/negatively charged regions. These molecules are said to be Polarised

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6
Q

What are Polymers?

A

Long chains of monomer sub-units

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7
Q

What is formed each time a monomer is added to a polymer chain?

A

a molecule of water/H2O

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8
Q

What is the formation of polymers called?

A

Polymerisation

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9
Q

What are reactions that produce water
called?

A

Condensation reactions

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10
Q

How are polymer chains broken down?

A

through the addition of water

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11
Q

What type of reaction involves the breaking down of polymers through the addition of water?

A

Hydrolysis

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12
Q

What do Polynucleotides (nucleic acids) hydrolyse to make?

A

Mononucleotides

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13
Q

What do Nucleotides make after condensation?

A

Polynucleotides (nucleic acids)

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14
Q

What do Polysaccharides (carbohydrates) hydrolyse to make?

A

Monosaccharides

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15
Q

What do Monosaccharides make after condensation?

A

Polysaccharides (carbohydrates)

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16
Q

What do fatty acids or glycerol hydrolyse to make?

A

Lipids

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17
Q

What do Lipids make after condensation?

A

Either fatty acids or glycerol

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18
Q

What do Polypeptides hydrolyse to make?

A

Amino acids

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19
Q

What do Amino acids make after condensation?

A

Polypeptides

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20
Q

What is the metabolism?

A

All the chemical processes in the body

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21
Q

What is a mole?

A

The SI unit for measuring the amount of a substance (abbreviated to mol)

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22
Q

How many particles are in one mole?

A

6.022x10^23

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23
Q

What is this number ,6.022x10^23, called?

A

Avagadros constant

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24
Q

What is a molar solution?

A

A solution with one mole of solute per litre of solution

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25
Q

What are Carbohydrates?

A

Carbon molecules combined with water, that range in size.

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26
Q

What are Organic molecules?

A

Carbon containing molecules

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27
Q

What is a significant feature of carbon atoms?

A

They readily form bonds with other carbon atoms, so can build up.

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28
Q

What is the most basic monomer unit in Carbohydrates?

A

A Sugar or Saccaride

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29
Q

What is a monosaccharide?

A

A single Saccharide monomer

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30
Q

What is a Disaccharide?

A

A Pair of Saccharides

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31
Q

What are Polysaccharides?

A

Monosaccarides combines in much larger numbers to make a chain.

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32
Q

What is the General formula for Monosaccarides?

A

(CH2O)n , n being any number from 3 to 7

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33
Q

Give three examples of Monosaccharides.

A

Glucose, Galactose and Fructose.

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34
Q

What are the two isomers of glucose?

A

α- glucose and β-glucose

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35
Q

What is a Reduction reaction ?

A

A chemical reaction involving the gain of electrons or hydrogen.

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36
Q

What is a Reducing sugar?

A

A sugar that can donate electrons to another chemical.

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37
Q

What is Benedict’s reagent?

A

an alkaline solution of copper (II) sulfate.

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38
Q

How do you test for reducing sugars?

A

The Benedict’s test

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39
Q

Describe Benedict’s test.

A

form a solution of food sample, add and equal amount of Benedict’s solution then heat in a water bath for five mins.

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40
Q

What colour would the Benedict’s reagent turn if a reducing sugar is present?

A

an orange brown colour

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41
Q

What two monosaccharides form the disaccharide maltose?

A

Glucose joined to Glucose

42
Q

What two monosaccharides form the disaccharide sucrose?

A

Glucose joined to Fructose

43
Q

What two monosaccharides form the disaccharide lactose?

A

Glucose joined to Galactose

44
Q

What is the bond formed between two monosaccharides after a condensation reaction?

A

a glycosidic bond between the two OH molecules

45
Q

What are non-reducing sugars?

A

saccharides that do not change colour of Benedict’s reagent they are heated with.

46
Q

Describe the test for non-reducing sugars.

A

complete Benedict’s test for reducing sugars, if it remains blue continue; hydrolyse solution with hydrochloric acid in a hot water bath; neutralise solution w/ sodium hydrogencarbonate; repeat Benedict’s

47
Q

Describe the test for starch.

A

add two drops of iodine to 2ml of solution; shake solution. If starch is present the solution would turn blue-black.

48
Q

Why are polysaccharides suitable for solution?

A

They are very large insoluble molecules.

49
Q

What is the structure of starch?

A

its made of chains of α-glucose, can be branched and unbranched and is wound into a tight coil that makes the molecule compact

50
Q

How is the structure of starch suited to its function?

A

large and insoluble, so doesn’t diffuse out cells; coils make it compact for storage; hydrolysed into α-glucose for respiration; is branched so can be easily acted on by enzymes, breaking it down quickly.

51
Q

Where is starch commonly found?

A

in plants such as potatoes, never found in animal cells.

52
Q

Describe the structure of Glycogen.

A

shorter chains of α-glucose that are highly branched.

53
Q

How does glycogen’s structure suit it’s function?

A

insoluble so doesn’t diffuse out cells or affect water potential; is compact; highly branched so eaisly broken down for resperation (animals have higher metabolic rate)

54
Q

Where is glycogen commonly found?

A

in animal and bacteria cells, but never in plant cells.

55
Q

How does the structure of cellulose majorly differ to glycogen and starch?

A

instead of α-glucose it uses β-glucose and forms straight unbranched chains

56
Q

Describe the structure of the cellulose chains

A

they run parallel to one another allowing hydrogen bonds to form cross-linkages between adjacent chains. goruped together they form microfibrils

57
Q

What is the structure of cellulose fibres?

A

Microfibrils are collected together and arranged in parallel groups of fibres.

58
Q

What do the hydrogen bonds in cellulose do?

A

the large number provides collective strength.

59
Q

Why is Cellulose’s structure suited to it’s function?

A

the straight unbranched chains; hydrogen bonds bring collective strength; grouping of microfibrils provides more strength.

60
Q

What is the function of Cellulose in a plant?

A

to provide support and rigidity

61
Q

What are common characteristics of lipids?

A

they contain carbon, hydrogen and oxygen in smaller proportion than carbs; insoluble in water ; soluble in organic solvents (alcohols and acetone)

62
Q

What are the main groups of lipids?

A

Triglycerides and phospholipids

63
Q

What are the roles of lipids?

A
  • cell membranes
  • source of energy (2x than carbohydrates)
  • insulation (slow conductors of heat)
  • waterproofing (insoluble, found on cuticle)
    -protection (stored around delicate organs)
64
Q

Describe the structure of Triglycerides.

A

three fatty acids combined with a glycerol, with three ester bonds

65
Q

What is a saturated fatty acid?

A

a fatty acid with no double bond between carbon atoms.

66
Q

What is an mono-unsaturated fatty acid?

A

a fatty acid with one double bond between carbon atoms

67
Q

What is an poly-unsaturated fatty acid?

A

a fatty acid with multiple double bonds between carbon atoms

68
Q

How does the structure of triglycerides suit their function?

A

have a high amount energy storing bonds so good source of energy; low mass to energy ratio; insoluble so doesn’t affect cell’s water potential; release water when oxidised, so important source of water

69
Q

What provides variation in triglycerides?

A

the variation of over 70 fatty acids

70
Q

Whats the structure of fatty acids?

A

a carboxyl group (COOH) with hydrocarbon chain attached

71
Q

Describe the structure of phospholipids.

A

two fatty acid and a phospholipid molecule connected to a glycerol molecules.

72
Q

What two parts is the phospholipid molecules split into?

A

a hydrophobic ‘tail’ - fatty acids
a hydrophilic ‘head’- phosphate molecule

73
Q

How does the structure of phospholipids suit their function?

A

polar so can form a bilayer as hydrophobic tail and hydrophilic tail; can form glycolipids at cell surface membrane

74
Q

How would you test a solution for lipids?

A

add solution and ethanol to a dry grease-free test tube. shake tube then add water. for a control test, use water as a solution.

75
Q

What is the result of a lipid test if a lipid is present?

A

a milky-white emulsion is formed

76
Q

What do polypeptide chains combine to form?

A

a Protein

77
Q

What are the four chemical groups in amino acids?

A
  • amino group (-NH₂)
  • carboxyl group (-COOH)
  • hydrogen atom (-H)
  • R group
78
Q

What bond is formed between two proteins?

A

a peptide bond between the carbon of the carboxyl group of one amino acid and the nitrogen of the amino group of the other

79
Q

What is the primary structure of a protein?

A

the sequence of amino acids found in its polypeptide chain

80
Q

Why does the primary structure of a protein affect it’s function?

A

the function of a protein depends on the shape, a single change in the primary structure could alter the bonds formed in the tertiary structure and thus proteins shape.

81
Q

What is the secondary structure of a protein?

A

the polypeptide chains form weak hydrogen bonds as amino acids are polarised, this causes the chains to twist into an α-helix coil.

82
Q

What is the tertiary structure of a protein?

A

the coiling, bonding and twisting of the α-helix polypeptide chain caused by disulphide bridges, ionic and hydrogen bonds

83
Q

What is the Quaternary stricture of a protein?

A

the combination of a number of different polypeptide chains and associated prosthetic (non-protein) groups into large complex protein.

84
Q

What is the test for protein called?

A

the Biuret test

85
Q

Describe the test for proteins.

A

place solution in a test tube with an equal amount of sodium hydroxide. then add a few drops of very dilute of. copper (II) sulfate solution.

86
Q

What colour would the solution turn in the Biuret test is protein is/isn’t present?

A

it will turn purple if peptide bonds (protein) are present, and will remain blue if not.

87
Q

What are the two basic molecular types of protein?

A

fibrous and globular proteins

88
Q

what are fibrous proteins? and give an example.

A

structural functions eg. collagen

89
Q

what are globular proteins? and give an example.

A

metabolic functions eg. enzymes and haemoglobin

90
Q

What are Catalysts?

A

chemicals that alter the rate of a chemical reaction without undergoing permanent changes to themselves.

91
Q

What are enzymes?

A

proteins that act as catalysts

92
Q

How do enzymes increase the rate of reaction?

A

they lower activation energy allowing reactions to take place at a lower temperature than normal

93
Q

What is the active site of an enzyme?

A

the functional depression on the molecule where the substrate binds and is acted on

94
Q

What is an enzyme-substrate complex?

A

the complex formed by the bonding between enzyme and substrate at the active site.

95
Q

What is the induced-fit enzyme model?

A

the enzymes active site slightly changes shape to bind with the substrate

96
Q

What factors affect the rate of enzyme controlled reaction?

A

Temperature, pH, substrate concentration, enzyme concentration and inhibitors

97
Q

How does a lower temperature affect the rate of enzyme reactions?

A

lower temp means not enough kinetic energy for substrate and enzymes to successfully collide.

98
Q

Why does the rate of reaction drop off when the temperature gets too high?

A

the enzyme denatures due to temperature

99
Q

How does significant changes in pH affect enzymes?

A

they could denature them

100
Q

What are the two types of enzyme inhibitor?

A

competitive and non-competitive inhibitors

101
Q

What is a competitive inhibitor?

A

an inhibitor that competes with the substrate to occupy the active site

102
Q

What is a non-competitive inhibitor?

A

an inhibitor that attaches to the enzyme molecule changing the enzymes shape and thus making it unable to form a substrate-enzyme complex.

Biology (11 decks)

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