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Biology > Chapter 1 > Flashcards

Chapter 1 Flashcards

1
Q

Define Monomer

A

A single repeating unit

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2
Q

Define polymer

A

A chain of monomers

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3
Q

Define hydrolysis

A

A reaction where you add water to break a bond

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4
Q

Define condensation

A

Joining molecules which releases water

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5
Q

Give 4 examples of carbohydrates

A

sugars starch cellulose glycogen

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6
Q

Define metabolism

A

all the chemical reactions that occur in cells or in an organism

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7
Q

Define isomer

A

A version of a molecule

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8
Q

Give the monomer of the following polymers Carbohydrates Lipids Proteins DNA

A

monosaccharides fatty acids and glycerol amino acids nucleotides

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9
Q

Give examples of monosaccharides

A

Glucose Galactose Fructose

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10
Q

Give examples of disaccharides and say what they are made up of

A

Maltose - glucose + glucose Sucrose - glucose + fructose Lactose - glucose + glacatose

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11
Q

Name the 2 glucose isomers

A

Alpha Beta

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12
Q

What test is used to test of reducing sugars

A

Benedicks + heat

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13
Q

What is used to test for starch?

A

Iodine solution

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14
Q

How many carbon atoms are in a Triose Pentose Hexose

A

3 5 6

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15
Q

Explain the test for non reducing sugars

A

add sucrose to test tube add hydrochloric acid place in boiling water for 5 minutes add sodium hydrogencarbonate to neutralise the acid test pH add benedicks to test tube place in boiling water for 5 minutes record results

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16
Q

State the test for non reducing sugars

A

Hydrolysis Benedicks + heat to boiling

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17
Q

What is a bond between two glucose molecules called?

A

Glycosidic bond

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18
Q

What are carbohydrates made up of?

A

Carbon Hydrogen Oxygen

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19
Q

General formula of monosaccharides

A

C(H20)

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20
Q

Starch is made up of long chains of ——- glucose linked by ————- bonds

A

Alpha Gylcosidic

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21
Q

Chains in ——- can be branched or ———— . ————- chains are wound into tight coils

A

Starch Unbranched Unbranched

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22
Q

What is a monomer of a protein?

A

An amino acid

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23
Q

What is a polymer of a amino acids?

A

A polypeptide

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24
Q

What is the generalised structure of an amino acid?

A

H

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25
Q

How many types of amino acids are there?

A

20

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26
Q

What is the bond in a polypeptide?

A

A peptide bond

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27
Q

What is the name for 2 amino acids bonded together?

A

Dipeptide

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28
Q

What is the solution used to test for proteins? What is this made of?

A

Biuret solution Sodium hydroxide and copper 2 sulphate

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29
Q

What are the colour changes in a biuret test?

A

Blue to lilac (if present)

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30
Q

What is the primary structure of a protein and what does it do?

A

It is the number and sequence of amino acids in a polypeptide chain that determines the shape and function of the protein

31
Q

What is the secondary structure - bonds and shape

A

Alpha helix coil Beta pleated sheet Hydrogen bonds

32
Q

What is the tertiary structure- bonds, shape, examples

A

Further folding and coiling of the protein to give a more complex and specific 3-D shape Hydrogen bonds Ionic bonds Disulphide bonds Globular proteins - enzymes

33
Q

What is the quaternary structure Bonds, examples structure

A

More than one polypeptide chain often with prosthetic groups Hydrogen bonds Ionic bonds Disulphide bonds Hormones - quaternary

34
Q

Enzymes are ———- at the ———— level . They are ————- proteins that act as —————- ————- to speed up reactions. Enzymes ——— the ————— energy required for a reaction

A

Proteins Tertiary Globular Biological catalysts Lower Activation

35
Q

What is the difference between the lock and key model and the induced fit model?

A

The lock and key model states that the substrate exactly fits into the enzyme but the induced fit model shows that the enzyme has to alter the active site in order to exactly fit the substrate.

36
Q

How does an enzyme break a substrate into product molecules?(induced fit model)

A

Puts stress on the bonds of the substrate which breaks them

37
Q

Name all the factors affecting enzyme action (6)

A

Temperature pH Substrate concentration Enzyme concentration Competitive inhibitors concentration Non competitive inhibitors concentration

38
Q

Name the 2 ways of measuring rate of reaction

A

The formation of the product The disappearance of the substrate

39
Q

Describe a temperature vs rate of reaction graph

A

As temperature increases so does the rate of reaction because the kinetic energy of the substrate increases, hence why enzymes at cooler temperatures are inactive. At 37 degrees the maximum of the graph is reached because it is the optimum temperature of the enzyme. Past 37 degrees the rate of reaction rapidly decreases because the enzymes are being denatured and the hydrogen bonds are being overcome by the heat and this means the shape of the active site is changed so the enzyme substrate complex cannot be formed

40
Q

Describe a pH vs rate of reaction enzyme graph

A

pH changes alters the number of free hydrogen and hydroxide ions, which will affect the charge on the amino acid and hence leads to the denaturation of the active site Beyond the optimum the charges of the amino acids and hence the proteins is changed which disrupts the active site

41
Q

Explain the affect of low enzyme concentration on the rate of reaction

A

There is a shortage of active sites because there are more substrate molecules than the enzyme, which means the substrate is in excess so there is a low rate of reaction

42
Q

Explain the effect of medium enzyme concentration on the rate of reaction

A

The addition of enzymes means that there is the perfect amount of enzymes for substrates so all the active sites are filled and the optimum concentration is reached

43
Q

Explain the effect of high enzyme concentrations on rate of reaction

A

As there are already enough active sites for all the substrate there is no additional effect of the extra enzymes

44
Q

Explain the difference between a substrate concentration graph and a enzyme concentration graph

A

The enzymes are the limiting factor for a substrate concentration graph whereas the substrates are the limiting factor on the enzyme concentration graph

45
Q

What do inhibitors do?

A

Slow down the enzyme rate of reaction

46
Q

What do competitive inhibitors do?

A

Take the place of the substrate as they have a similar shape and then makes an enzyme inhibitor complex not a substrate enzyme complex so it slows down the rate of reaction

47
Q

What do non competitive inhibitors do?

A

Change the shape of the active site by binding to another place in the enzyme which prevents the substrate from fitting so that means no enzyme substrate complex is formed

48
Q

What are lipids made of?

A

Hydrogen carbon and oxygen

49
Q

Are lipids soluble or insoluble in water?

A

Insoluble

50
Q

Are lipids soluble or insoluble in ethanol?

A

Soluble

51
Q

Name 4 roles of lipids

A

Source of energy Waterproofing Insulation Protection

52
Q

Explain why lipids are good insulators

A

They have slow conduction of heat

53
Q

Explain why lipids are good sources of energy

A

They have double the energy of carbohydrates

54
Q

Explain how lipids are used for protection

A

They store fat around delicate organs for protection

55
Q

What are triglycerides made from?

A

1 glycerol molecule and 3 fatty acid molecules bonded by an ester bond

56
Q

What is a saturated fatty acid?

A

A fatty acid with no double carbon bond where there are as many atoms as there can be

57
Q

Define mono-unsaturated

A

A fatty acid with only 1 double carbon bond which means only one more atom can be added

58
Q

Define a polyunsaturated fatty acid

A

A fatty acid with 2 or mote double carbon bonds where many atoms could be added

59
Q

Fatty acids are _____ or uncharged, hydro________ molecules

A

Non polar Hydrophobic

60
Q

Describe the structure of a triglyceride:

A

Compact and good for storage Insoluble in water Excellent source of energy Fat source of metabolic water

61
Q

What bond is formed between glycerol and fatty acids

A

Ester bond

62
Q

What is a phospholipid made of

A

2 fatty acids, 1 phosphate group and 1 glycerol

63
Q

Phospholipids are __________ but they have a phosphate head which is ——— and is hydrophilic

A

Non polar Polar

64
Q

Chains in ——- can be branched or ———— . ————- chains are wound into tight coils

A

Starch Unbranched Unbranched

65
Q

Explain 4 advantages of the structure of starch

A

They are large and insoluble so they dont diffuse out of the cell and dont affect the water potential of the cell Compact so a lot can be stored in small spaces When hydrolysed they make alpha glucose which is used for respiration and is easily transported The branched form has many ends which can be acted on by enzymes simultaneously

66
Q

Explain the difference between the structure of starch and glycogen

A

Glycogen is more highly branched and makes shorter chains

67
Q

Where is glycogen stored in animals

A

Liver and muscles

68
Q

Explain 4 advantages of the structure of glycogen

A

Insoluble so it doesn’t dissolve out of cells Compact Can be broken down rapidly bc highly branched- produces alpha glucose which is good for animals with high metabolic rates Insoluble so it doesn’t affect water potential

69
Q

What glucose is cellulose made of

A

Beta

70
Q

Does cellulose form straight unbranched chains or branched coil chains

A

Straight unbranched chains

71
Q

What bonds form between the chains for cellulose? What is the use of these?

A

Hydrogen chains Add to overall strenght

72
Q

When cellulose is grouped together what does it form?

A

Microfibrils

73
Q

When grouped together what do microfibres form

A

Fibre

74
Q

Explain 3 advantages from the structure of cellulose

A

Strong bc of hydrogen cross linkages Form straight unbranched chains which are strong Molecules group to make fibres which add even more strength

Biology (21 decks)

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