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Biology Unit 2 > module 1 > Flashcards

module 1 Flashcards

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1
Q

What’s are substances taken into the body used for/in?

A

Metabolism

Digestion -then rebuilt ti form different parts of the organism

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2
Q

What happens if a substance can’t do this

A

Removed from body

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3
Q

Talk about fibre as an example

A

Doesn’t provide nutrients but is essential component of the duet cz it helps in flow of materials through the gut
Also helps remive waste products
Lack if it could lead to intestinal cancer

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4
Q

Name the 6 chemical groups

A 
Carbohydrates
Vitamins & minerals
Water
Nucleic acid
Lipids
Proteins
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5
Q

What’s carbs for

A

Energy storage & supply

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6
Q

Proteins for?

A

Enzymes & hormones, antibodies/antigens, structure

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7
Q

Lipid s

A

Membranes, thermal insulation, electrical insulation in neurones

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8
Q

Vitamins & minerals

A

Act as coenzymes (some)

Take part in metabolic reactions

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9
Q

Nucleic acids

A

Info molecules

Carry instructions for life

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10
Q

Water

A

Take part in many reactions
Support in plants
Medium in many reactions
Transport

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11
Q

What are the key biological molecules

A

Carbohydrates
Proteins
Lipids
Nucleic acids

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12
Q

What are the chemical elements found in biological molecules

A

Carbon
Hydrogen
Oxygen
Nitrogen

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13
Q

Whys water described as a biological molecule sometime?

A

Cz of its important role to life

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14
Q

What is biochemistry

A

Chemical reactions that involve biological molecules

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15
Q

What is metabolism

A

Sum total of all the biochemical reactions taking place in the cells of an organism

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16
Q

What are catabolic reactions

A

Breaking down larger molecules to smaller ones

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17
Q

What are anabolic reactions

A

Building smaller molecules into larger ones

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18
Q

Examples of catabolic & anabolic

A

Digestion catabolic

Muscle growth anabolic

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19
Q

Why is carbon a kind of frame - work atom

A

Cz of its multiple - bonding feature
Can bond with other carbon atoms for longer chains & rings
Can bond with other atoms yo form molecules with different properties & structures

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20
Q

What is a risk factor

A

Factor that increases your chances if developing a particular disease

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21
Q

What is a covalent bond

3 points

A

When electrons are shared between atoms
They’re strong
Covalently bonded atoms form new molecules

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22
Q

Hiw many covalent bond can carbon form

A

4

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23
Q

Why can carbon form form a vast variety of molecules

A

Cz it can bond to other carbon atom to produce longer chains & rings and other atoms to produce molecules with different properties and structures

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24
Q

2 examples if carbon double bonds

A

C=c

C=o

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25
Q

Why are lipids not polymers?

A

Cz the monomers are very different from each other

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26
Q

What reaction links monomers together. Also includes lipids

A

Condensation reaction

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27
Q

3 steps of condensation reactions

A

Water molecules released
Cove Kent bond formed
Larger molecule formed by binding of smaller ones

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28
Q

What’s the chemical reaction that splits larger molecules

A

Hydrolysis reaction

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29
Q

3 steps of hydrolysis reaction

A

Water molecule used
Covalent bond broken
Smaller molecules formed by splitting of larger molecule

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30
Q

When do hydrogen bond form

A

When a slightly negatively charged part of a molecules comes close to a slightly positively charged hydrogen atom in same or other molecule

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31
Q

Strength of hydrogen birds?

A

Not strong

But if many form eg in polymers it stabilises the structure

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32
Q

Function of carbohydrates in organisms

4 points

A

Store energy (starch)
Source of energy (released from glucose during respiration)
Structure (cellulose)
Also form part of larger molecules (nucleic acids & glycolipids)

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33
Q

Elements are found in what proportion in carbs

A

Cn (H2O) n

For every carbon present equal number of water molecule present too

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34
Q

Monomer of carbohydrates?

A

Monosaccharides

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35
Q

3 properties of monosaccharides

A

Soluble in water
Sweet tasting
Form crystals

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36
Q

3 carbon monosaccharides called?

5 & 6 too?

A

Triose
Pentose
Hexose
Sugars

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37
Q

What are most common monosaccharides

Give 2 examples

A

Hexose Sugars

Glucose & fructose

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38
Q

Structure of Pentose & Hexose Sugars?

A

Ring structure

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39
Q

What are the 2 forms of glucose?

A

Alpha and beta

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40
Q

Difference is true tyre between alpha glucose and beta glucose

A

Alpha has its OH at C1 below the plane of the ring

Beta has its OH at C1 above the plane of the rjng

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41
Q

2 monosaccharides in condensation reaction firm what?

A

Disaccharide molecule

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42
Q

Type if bond formed and specific name of bond when disaccharide is formed
What happens to water

A

Covalent bond
Glycosidic bond
Water is eliminated

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43
Q

Are disaccharides sugars?

A

Yes

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44
Q

What are the 2 products of a condensation reaction?

A

Polymer

Water molecule

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45
Q

What releases energy in respiration?

What can this energy be used for?

A

Breaking down of glucose to water and carbon dioxide

To make ATP

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46
Q

Respiration equation

A

Glucose + oxygen –> carbon dioxide + water + energy used to form ATP

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47
Q

How can you ensure you can use glucose in respiration?

A

Using specific enzymes in each step

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48
Q

Animals and plants break which type of glucose only?

A

Alpha

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49
Q

Why can’t animal and plant enzymes break down beta glucose?

A

Because of the different arrangements of the H and OH atoms at C1

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50
Q

Why can animals and plants only use alpha glucose not beta for respiration?

A

Because the enzymes function is based on shape.

Shape of alpha is different to shape of beta do same enzymes can’t break both

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51
Q

What do 2 alpha glucose form

What if you keep bonding them together what does that form?

A

Maltose

Amylose

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52
Q

Where does the Glycosidic bond between all the glucose subunits occur?
2 points

A

Carbon number 1 of one molecule and carbon number 4 of another hence the 1,4-Glycosidic bond

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53
Q

What causes the Amylose chains to coil

A

The shape of the glucose molecules and the formation of Glycosidic bonds

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54
Q

How does coiling affect the structure of Amylose

A

Makes it compact

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55
Q

What is trapped in the coils of the spring of Amylose

A

Iodine molecules

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56
Q

What causes iodine to change colour to from yellow/brown to bkue/black in the starch test?

A

The fact that iodine molecules are trapped in the coils of the spring of Amylose

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57
Q

Difference between Amylose and similar molecules ti glucose molecules

A

Thwy aren’t water soluble

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58
Q

Starch in what organisms?

A

Plants

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59
Q

Structure of starch

3 points

A

Made of alpha glucose molecules that have bonded together
Made of Amylose
Made of amylopectin

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60
Q

Where is starch stored in plants?

A

Chloroplasts

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61
Q

Why is starch a source of energy

A

Starch can be broken down to glucose molecules which can be respired down to release energy

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62
Q

Glycogen in what organisms

A

Animals

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63
Q

How is glycogen similar to starch?

A

Made of alpha glucose molecules

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64
Q

How us glycogen different to starch

A

Glycogen is branched

Starch is straight chained

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65
Q

How is glycogen different to amylopectin

How does this show difference to starch?
3 points

A

1-4 Linked glucose chains in glycogen are shorter
Have more branches
So glycogen is more compact than starch

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66
Q

2 features of glucose and starch

Explain further

A

Don’t dissolve
So the stored glucose doesn’t affect the water potential of the cell

They hold glucose molecules in chains
This means they can easily be broken off from the ends to provide glucose for respiration

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67
Q

What catalyses condensation and hydrolysis reactions

A

Enzymes

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68
Q

How us beta glucose different to aloha glucose when they condense

A

In beta glucose the resulting chain is straight and long

In alpha glucose the chain is coiled and spring-like

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69
Q

What are beta glucose polymer chains called

A

Cellulose

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70
Q

Which are stronger cellulose or Amylose

A

Cellulose

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71
Q

Which organism is cellulose only found in

And where

A

Plants

Plant cell walls

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72
Q

Why are many hydrogen bonds formed between glucose monomers in cellulose

A

Cz they contain a lot of OH groups

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73
Q

Describe the cellulose chain

A

Beta glucose units in cellulose chain
Hundred of chains = microfabric linked by hydrogen bonds
Microfibrils held together by hydrogen bonds to form macrofibrils

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74
Q

Mechanical strength of macrofibrils

A

Strong close to that of steel

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75
Q

Where are macrofibrils embedded, to form what?

A

Embedded in pectin to form cell walls

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76
Q

Structure and function of plant cell wall

4 points

A

Cell walls around plant cells give strength to cell, supporting the whole plant
Arrangement of macrofibrils allows water to move through and along cell walls and water can pass in and out of the cell easily
Walls prevent cell to burst, in turgid plants it helps to support the whole plant
Cell walls can be reinforced with other substances to provide extra support

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77
Q

2 different types of structural carbohydrate than cellulose

And info

A

Chitin and peptidoglycan
Chitin = forms exoskeleton of insects
Peptidoglycan = is the basis of cell walls found around most bacterial cells

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78
Q

What is cellulose

A

A carbohydrate polymer made by bonding beta glucose molecules

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79
Q

Why do differences between starch and cellulose occur

A

Cz of the difference between alpha glucose and beta glucose
The OH at C1 is below the plane of the ring in alpha glucose
The OH at C1 is above the plane of the ring in beta glucose

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80
Q

Functions of proteins

5 points

A

They are membrane carriers and pores (in active transport and facilitated diffusion)
All enzymes are proteins
Many hormones are proteins
Antibodies are proteins
They’re structural components (of muscle and bone)

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81
Q

Overall importance of proteins

2 points

A

Provide growth and repair

Crucial to most metabolic activity

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82
Q

Monomers that make proteins?

A

Amino acids

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83
Q

Basic Structure of all amino acids?

A

Amino group, acid group and carbon in between and an r group

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84
Q

What causes the difference in structure and properties in amino acids if their basic Structure if very similar?

A

The different r groups

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85
Q

How mant naturally amino acids are there

A

20

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86
Q

How can r groups differ?

A

Some are positively charge some are negatively charged

Some are hydrophobic some are hydrophilic

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87
Q

How do plants manufacture amino acids

A

Nitrate from the soil is converted to amino groups and bonded to organic groups made from the products of photosynthesis

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88
Q

Difference of amino acids in plants and animals

A

Plants manufacture them

Animals take in port wins to obtain amino acids

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89
Q

How do animals get amino acids

A

The proteins they take in are digested to amino acids and other proteins can be built from these amino acids

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90
Q

What are essential amino acids

A

They are an essential part of the diet

They can’t be built from materials taken into the organisms body

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91
Q

Hiw many of the naturally occurring amino acids are essential acids in animals

A

8-10 out of 20

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92
Q

Why should vegetarians be careful with their diet I terms of amino acuds

A

Because most essential amino acids are found in meat not plants. So they need to balance their diet properly

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93
Q

Why can’t animals store excess amino acids

A

Because the amino group makes them toxic

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94
Q

Hiw is the amino group removed
Where does this take place?
What is the amino group converted to?
Where is it removed?

A

Deamination
Liver
Urea
Urine

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95
Q

Where is the covalent bond formed in amino acids

A

The amino group of one amino acid and the acid group of another amino acid

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96
Q

What is the covalent bond called that bonds amino acids

A

Peptide bond

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97
Q

What are the 2 products formed in a condensation reaction of 2 amino acids

A

Peptide bond and water molecule

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98
Q

Why is the making and breaking of peptide bonds important

2 points

A

Building and rebuilding of protein molecules

Breaking down proteins ti amino acids for example in digestion

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99
Q

What is it called when many amino acids join together not just 2

A

Polypeptide

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100
Q

Why are amino acids in a polypeptide chain referred to as amino acid residues

A

Cz part of the molecule is lost in the condensation reaction that produces the peptide bond

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101
Q

Where in a cell are polypeptides made?

A

Ribosomes

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102
Q

What process makes polpeotude/proteins

A

Protein synthesis

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103
Q

From what molecule is info used to form polpeptides/proteins

A

mRNA

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104
Q

Briefly describe process of protein synthesis

4 steps

A

mRNA Passes through the ribosome
Amino acids join are joined together one at a time
Peptide bond formed after a condensation reaction
This produces a linger chain of amino acids

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105
Q

What determines the sequence of amino acids

A

The mRNA

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106
Q

How do you make sure you can make different types of proteins

A

Make sure different mRNA molecules pass through ribosomes

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107
Q

What do all proteins have at each end

A

An amino group and an acid group at the other end

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108
Q

What determines the function of a protein

A

It’s primary structure (it’s amino acid seqyence)

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109
Q

How do you calculate the total number of different possibilities of amino acid sequences?
4 amino acid polypeptide chain example

A

E.g. A polypeptide chain with 4 amino acids

20x4 = 160000 different sequenced of four amino acids are possible

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110
Q

Why is the formation and breakage of covent bonds uses enzymes to catalyse the reactions

A

Cz covalent bonds are very strong, they can’t just appear or fall apart

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111
Q

What are the enzymes called that catalyse the breaking of peptide bobds

A

Protease enzymes

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112
Q

Examples of when organism break down and rebuild proteins

A

Digestion
Hormone regulation
Ageing

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113
Q

Why does hormone regulation (break down) occur

A

So that their effects aren’t permanent and can be controlled

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114
Q

Why does skin lose its elasticity and become wrinkled - ageing

A

Cz older skin is less able to rebuild the protein collagen that gives skin it’s smooth and elastic properties

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115
Q

How do coils and pleats in amino acid chains help

A

They help avoid tangling and breaking

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116
Q

What holds the coils and pleats on place

A

Hydrogen bonds

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5
Perfectly
117
Q

What does the amount of coiling and pleating in a chain depend on

A

The types of amino acids being added to the chain (primary structure)

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118
Q

What is the primary structure of a protein

A

The sequence of amino acids

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119
Q

What is the secondary structure of proteins
What holds the coils in place
Although they’re weak how do they help?

A

When an alpha helix is formed die to the coils and pleats
Hydrogen bonds hold the could in place
There are many hydrogen bonds, so their overall effect is stability for the chain

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120
Q

What is the tertiary structure of a protein

What holds its shape at this stage?

A 
It's the 3D shape of a protein
When the coils and pleats themselves coil or fold
4 bonds - disulfide
Hydrogen
Ionic
Hydrophobic and hydrophilic interactions
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121
Q

What forms hydrogen bonds in tertiary structure of a protein

A

When a negatively charged groups are found near positively charged groups

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122
Q

What lead to the formation of ionic bonds in proteins

A

R groups sometimes carry a charge

When oppositely charged amino acids are found close to each other

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123
Q

What causes a disulfide bond in proteins

A

When two cysteines are found close to each other -they contain sulfur

124
Q

What determines a proteins function

Examples of importance of structure for function

A

It’s tertiary structure
Hormones must be a specific shape to fit into a receptor
An enzyme must have the right active site shape that is complimentary to its substrate

125
Q

Effect of heat on tertiary structure of proteins

A

Kinetic energy increases in the molecule
Causes molecule to vibrate
This causes some of the weaker bonds not including covalent or disulfide bond to break
With enough heat, the entire tertiary structure can be unravelled which stops the protein from functioning well
It becomes denatured

126
Q

What are the 2 main categories of 3D shape of proteins

A

Globular and structural proteins

127
Q

3D Feature
Solubility in water
Role
Example of globular proteins

A

Roll up to form balls
Soluble mainly
Usually metabolic roles
Enzymes & antibodies

128
Q

3D features
Solubility in water
Role
Example of fibrous proteins

A

Form fibres
Insoluble usually
Structural roles
Collagen in bone and cartilage/keratin in hair and nails

129
Q

What does a quaternary structure of a protein mean

A

It has more than one polypeptide subunit or has an inorganic component with a polypeptide

130
Q

2 examples of protein with a quaternary structure

A

Insulin and haemoglobin

131
Q

How many polypeptide chains does haemoglobin have
Types of chains in the 4 chains
Type of protein
Water solubility

A

4
2 alpha chains and 2 beta chains
Globular
It’s soluble in water

132
Q

Function of haemoglobin

A

Carry oxygen from the lungs to the body tissues

133
Q

What is the prosthetic group found in haemoglobin

A

Haem group

134
Q

What are prosthetic groups

A

Groups that aren’t amino acids but are an essential part of a protein

135
Q

What is responsible for the colour of haemoglobin

A

The haem group

136
Q

What does haem groups contain that binds to oxygen

A

(Fe2+) iron ion

137
Q

How many oxygen molecules can bind to one haemoglobin to be transported to body tissues from lungs

A

4
4 haem groups
4 iron ion groups that bind to oxygen

138
Q

Structure if collagen:
What type of protein is it
How many polypeptide chains is it made out of
How does it look like
What happens to the 3 chains
What gives the structure of collagen strength, between what?

A 
Fibrous
3
A twisted rope
Theyre coiled
Hydrogen bonds,  between the chains
139
Q

What increases the strength of the collagen molecule further?

A

The formations of covalent bonds (cross-links) with other collagen molecules

140
Q

What are the stages of collagen strength? 3 points

A

Collagen cross-links with other collagen molecules
This forms fibrils
Which forms fibres

141
Q

Function of collagen

And 5 examples

A

Provides mechanical strength

Walls of arteries - prevents walls from bursting due to high blood pressure

Tendons - they’re mostly collagen and form a strong connection that allows muscles to pull bones

Bones are made from collagen, this makes them hard

Cartilage and connective tissue made from collagen

Cosmetic treatments - colkagen ibjected into lips, used to give fuller lips

142
Q

What is a solid lipid and a liquid lipid called

A

Fat

Oil

143
Q

Functions of lipids

6 functions

A

Electrical insulation around neurones

Some hormones are lipids

Source of energy (lipids can be respired like glucose to release energy to generate ATP)

energy storage in adipose cells

All biological membranes arw made from lipids

Waxy cuticle of plant leaves - helps prevent them from drying out

144
Q

Solubility of lipids in water

A

Insoluble

145
Q

Where are glycerol and fatty acids found

2 places

A

All lipids that perform energy storage and supply and those found in membranes

146
Q

Is it fatty acid molecules or glycerol molecules that differ

A

Fatty acids

Glycerol molecules stay the same

147
Q

What are essential fatty acids

A

Fatty acids that can’t be made by animals

They need them from raw materials

148
Q

How are fatty acids similar but very different

A

They always have the same acid group

But their hydrocarbon chain differs (can be 2-20 carbons long)

149
Q

What do saturated and unsaturated fat refer to?

A

Whether the hydrocarbon chain is saturated with hydrogen or not

150
Q

What are unsaturated fatty acids

2 points

A

Fatty acids that c=c bonds

So fewer hydrogen atoms can be bonded to the molecule

151
Q

How can you predict whether a lipid is oil or fat

A

Oils tend to have many unsaturated fatty acids cz the many c=c bonds changed the shape of the hydrocarbon chain which makes it more fluid

Fats are more saturated and don’t have a major change to their hydrocarbon chain cz of lack of c=c bonds so they aren’t very fluid

152
Q

What type of lipid is animals lipid

What about plant lipid

A

Solid/Fat e.g. lard

Liquid/Oil e.g. olive oil

153
Q

What is a triglyceride made out of

A

One glycerol molecule and 3 fatty acids

154
Q

Where does the condensation reaction occur that forms triglycerides

A

Between the acid group if a fatty acid molecule and an OH group if the glycerol molecules

155
Q

What type and name of bond is formed between the condensation reaction between a fatty acid and a glycerol

A

Covalent bond

Ester bond

156
Q

What are the 2 molecules produces after a condensation reaction between a fatty acid and a glycerol

A

A water molecule and a mono/di/triglyceride

157
Q

Why are triglycerides hydrophobic/ water insoluble

3

A

Cz the charges on the molecules are dirtied evenly across the molecules
This means that the hydrogen bonds can’t form with water molecules
So the two types of molecules don’t mix together

158
Q

What CAN lipids dissolve in

A

Alcohol

159
Q

Examples of lipids

5 points

A 
Fatty acids
Triglycerides
Cholesterol
Phospholipid
Glycolipids
160
Q

How is a phospholipid molecule similar to a triglyceride molecule

A

Contains fatty acids and glycerol that are bonded together by a condensation reaction to produce an ester bond

161
Q

How is phospholipid formation different to triglyceride formation

A

In a phospholipid the 3rd fatty acid doesn’t bond to the OH group, instead a phosphate group bonds to it
It’s a covalent bond which also releases water

162
Q

Features of the heads and tails of phospholipids

A

Head is hydrophilic

Tail is hydrophobic

163
Q

What allows phospholipids to form membranes

A

The water solubility of their heads

164
Q

Fatty acids of phospholipids can be in saturates or saturated

How does this help

A

Allows organism ti control the fluidity of membranes

165
Q

Hiw does respiration of lipids occur

3 points

A

The ester bonds holding the fatty acids and glycerol are hydrolised by using a water molecule
Both glycerol and fatty acids can be further broken down into water and carbon dioxide
This releases energy which is used to generate ATP

166
Q

Which hives more energy and by hiw much

Respiration of one gram of carbohydrates or lipid

A

Lipid

Twice as much energy

167
Q

Why are lipids excellent energy storage molecules

A

They’re stored in a compact way and don’t affect water potential of the cell cz they’re insoluble in water

168
Q

What type is chokestrol

A

Lipid

169
Q

What is cholesterol made out of, not like triglycerides and phospholipids

A

4 carbon based rings

170
Q

What is its function in the membrane due to its hydrophobicness

A

Can sit in between phospholipid hydrocarbon tails

Regulated fluidity and strength of the membrane

171
Q

Examples of things made from cholesterol

A

Hormones testosterone and oestrogen

Vitamin D

172
Q

How does the lipid nature of steroid hormones help them in their functions

A

Can pass through the phospholipid bilayer easily to reach target receptor and can pass the nuclear envelope

173
Q

Example of where cholesterol is formed

A

Liver cells

174
Q

Why excess cholesterol can be harmful

2 examples

A

In the blood:

Cholesterol can be deposited in the inner lining of blood vessels causing atherosclerosis which can result in CHD

In bile:
Cholesterol can stick together to form gallstones

175
Q

Why and how is the genetic disorder hypercholeserolaemia bad

A

Cz cells manufacture and secrete too much cholesterol
This happens cz the cells don’t obey the signals to stop cholesterol production as they lack a particular cell surface receptor

People can die at 2 years of age

176
Q

What 3-2 forms do nucleic acids come in

A

DNA

RNA

177
Q

What do dna and RNA hold?

A

Coded info to build that organism

178
Q

Where is dna found in a eukaryotic cell

A

Nucleus

179
Q

Where is RNA found

A

In 3 different forms

180
Q

What os the monomer of all nucleic acids

A

Nucleotide

181
Q

What makes up a nucleotide

3 subunits

A

Organic nitrogenous base
Phosphate group
Sugar molecule

182
Q

What bond is used to join the 3 sub units

A

Covalent bond

183
Q

Variations of a phosphate group in nucleic acuds

A

None

They’re always the same

184
Q

Variation of sugar molecule in nucleic acuds

A

Either deoxyribonucleic sugar

Or ribose sugar

185
Q

Variation of organic nitrogenous bases in nucleic acids?

A 
Adenine
Guanine
Thymine
Cytosine
Uracil
186
Q

What join together in a condensation reaction to form a chain of nucleotides

A

The sugar molecule of one nucleotide with the phosphate group of another

187
Q

What consist of the backbone of nucleic acids

A

Phosphate group and sugar molecule

Base projects from them

188
Q

What forms coded info in nucleic acids

A

The sequence of bases

189
Q

Can ribose bond with deoxyribose
Why
So what?

A

No
Cz they aren’t the same sugar
So it’s either RNA or DNA

190
Q

How many pyramidines

Hiw many purines

A

3 pyramidines

2 purines

191
Q

What are the 3 pyramidines

A

Thymine Uracil

Cytosine

192
Q

What are the 2 purines

A

Adenine

Guanine

193
Q

How do pyramidines and purines differ

A

Pyramidines are smaller

194
Q

What causes gout

A

Too much nucleic acids (uric acid)

195
Q

Nucleotide monomers produce what type of monomer

A

Polynucleotide

196
Q

How is a dna molecule formed after a polynucleotide is formed

A

When 2 polynucleotide stands come together

197
Q

What strengthens the rungs of the ladder by forming bonds between the bases

A

Hydrogen bonds

198
Q

How do hydrogen bonds help in dna

A

Give it a stable structure

199
Q

Why is it vital for dna to have a stable structure

A

Because it holds instruction for life and to make an organism. Of unstable instruction would go wrong too easily

200
Q

Why is the term anti parallel used in dna crap

A

Because the dna strands run in opposite direction to each other
The sugars are pointing in opposite directions

201
Q

Why are the chains always the same distance apart

A

Cz of the way the nitrogenous bases pair up

Purines with pyramidines

202
Q

What forms between the bases when they cones together

A

Hydrogen bonds

203
Q

What is the base pairing described as

A

Complementary

204
Q

What is the final structure of a dna molecule known as

How does it form

A

Double helix

Twisting of the strands

205
Q

When does dna replication take place

A

Interphase

206
Q

What does dna replication create

A

Identical sister chromatids

207
Q

How do you make a new copy of a dna molecule

5 steps

A

Untwist double helix

Hydrogen bonds between base pairs broken which makes them exposed
Dna unzips

Free dna nucleotides are bonded by hydrogen bonds to the exposed bases

Covalent bond formed between phosphate group of one nucleotide and sugar molecule of another to seal the backbone

This continues until 2 new dna molecules are formed

208
Q

Why is it called semi conservative replication

A

Because each new dna molecule consists of one conserved strand and one new strand hence semi

209
Q

4 ways RNA is structurally different to dna

A

Only has one strand

Uracil rather than thymine

Ribose sugar not deoxyribose

3 forms of RNA molecules exist

210
Q

What can RNA molecules do/be due to the base pairing rules

(Basis of copying the genetic code of the dna base sequence) transcription

A

They can be complementary to dna

So they can bond to exposed Dna nucleotides

A chain of RNA nucleotide is then formed (transcription)

211
Q

What are the 3 forms of RNA molecules

A

tRNA
mRNA
rRNA

212
Q

What is an mRNA

A

It’s a copy of the coding strand of the dna molecule

Complementary ti the template strand

213
Q

What is rRNA

A

Found in ribosomes

214
Q

What is tRNA

A

Carries amino acids to ribosomes where they are bonded together to form polypeptides in protein synthesis

215
Q

Briefly explain protein synthesis in 7 steps

A

Sequence of bases code for particular protein molecules

They code for the sequence of amino acids in the protein

Hydrogen bonds split to expose a gene with this coding

RNA nucleotides form a complementary strand mRNA (which is a copy of the DNA coding strand or the gene

The mRNA peels away from the dna and leaves through a nuclear pore

mRNA attaches to a ribosome

tRNA bring amino acids in correct order to ribosomes, according to the base sequence on the mRNA

Amino acids joined together by peptide bonds to give a specific primary structure which gives rise to the secondary and tertiary structure

216
Q

What is a gene

A

Length of dna that codes for a polypeptide

217
Q

What does a gene occupy

A

Locus - a specific place on a chromosome

218
Q

What is an allele

A

Different version of the same gene

219
Q

How are all enzymes similar?

5 ways

A

Globular proteins
Soluble in water

Act as catalysts

Affected by pH and temperature

Have an active site

Specific

220
Q

What determines enzymes function

A

It’s shape and amino acid sequence

Primary, secondary and tertiary structures

221
Q

What is an active site

A

Area of an enzyme where catalytic activity of the enzyme occurs

222
Q

What does it mean that the active site of an enzyme is very specific

A

The reaction an enzyme can catalyse is also very specific

223
Q

What is a catalyst

A

A molecule that speed up chemical reaction s but isn’t used up in the reaction. The catalyst remains unchanged at the end of the reaction

224
Q

Advantage of enzymes over inorganic catalysts

A

As biological catalysts they aren’t used up and don’t produce waste product (unwanted byproducts)

225
Q

Metabolic reaction that are enzyme driven

A 
Glycosidic bond
Ester bonds
Peptide bonds
Protein synthesis
Respiration
Photosynthesis
Digestion
226
Q

What happens to a substrate in a reaction catalysed by an enzymes

An example

A

The substrate turns into a product

E.g. maltose hydrolysed into 2 glucose molecules with the enzyme maltose as the catalyst of the reaction

227
Q

What is sucrose made out of

A

Glucose and fructose

228
Q

What is an enzyme

A

Protein molecule that acts as a biological catalyst

229
Q

What happens if the shape of an enzyme changes

A

It’s can’t function/ work

230
Q

What makes an organism adapted to live in extreme environments

A

Their enzymes con it ie to function

231
Q

What does it mean to be able to regulate core body temperature independently (endothermic)

A

Enzymes can function at near optimum temperature

232
Q

Disadvantage and advantages of having enzyme activity

A

Dis
Using too much energy
More food need cz it components are used up

Adv
Allows organism to survive well by helping it live in more extreme environment

233
Q

3 examples of where enzymes can be found

A

Heterotrophs break down the body of organism they’re consuming in order to extract the nutrient molecules they need

In digestion. Catabolic reaction that break down larger molecules into their subunits (Glycosidic bonds, ester bonds, peptide bonds)

Some organism secrete enzymes onto the food source. They digest the molecules into their monomers

234
Q

What are extracellular enzymes

Example

A

Enzymes that are released from the cells that makes them

Eg 3 Nymet in digestive system

235
Q

What are intracellular enzymes

A

Enzymes that have their catalytic action take place inside the cells that make them

236
Q

How can enzymes be useful in protecting an organism

Example

A

They can help break down the molecules that may be harmful to the organism

Phagocytosis
Lysosome enzymes are used to digest bacteria that are engulfed by a phagocyte

237
Q

What is activation energy

A

The amount of energy that is need to enable the reaction to take place

238
Q

What’s the level of activation energy

A

It depends on reaction

239
Q

What role do enzymes play in activation energy

A

They reduce the amount of activation energy need to proceed with the reaction

240
Q

How can we allow metabolic reaction to take place without damaging the cells Involved

A

Use enzymes as catalysts

241
Q

What would happen if enzymes didn’t exist

A

Metabolic reaction would occur much slower to even maintain life

242
Q

What relations does the shape of active site have with substrate

A

They’re complementary to each other

243
Q

Why is it called the lock and key hypothesis

A

Because the substrate usually small, fits into the active site

244
Q

What is the induced fit hypothesis

A

The idea that changes to the enzyme occur as the substrate binds to the active site

Charges on the amino acids on the active site also contribute in the holding of the substrate molecule so that the reaction can proceed

245
Q

What happens if the substrate molecule is no longer held in active site

A

Reaction cannot occur

246
Q

7 steps of the induced fir hypothesis

A

Enzyme molecule changes shape slightly once a substrate molecules bond with the active site

This makes the active site fit the substrate better
Charge on active site also hold substrate in place (oppositely charged groups from active site and substrate) (enzyme substrate complex)

Change in enzyme shape also places strain on thus destabilise the substrate molecule which makes the reaction occur more easily

This produces a product (enzyme-product complex)

Product(s) are a different shape from substrate molecule

Product(s) no longer fits into active site so it moves away

Enzyme able to catalyse SAME reaction with another substrate molecule

247
Q

Which type of molecules have natural kinetic energy

A

Liquids and gas

248
Q

What happens if gas or liquid is heated

4 things

A

An increase in kinetic energy

Molecules vibrate and move aroubd more

They collide more often

They collide at a greater speed and force

249
Q

What lead to collision if active sit and substrate

A

Random movements of substrate and enzyme

250
Q

What happens if you increase temp in substrate and enzyme

5 things

A

Higher kinetic energy

Move around more

More likely to collide

Increased reaction rate

Increased number of products at a given time

251
Q

Example and steps of how enzymes van be denatured

7 steps

A

Increasing heat

More vibration

Vibrations cause weaker bond eg hydrogen and ionic bonds to break (which hold tertiary structure and maintain active site shape)

Thus alters it’s active sit shape

Rate of reaction decreases

Enzyme will stop function with increased heat

Structure too damaged to function so it’s irreversible and becomes denatured

252
Q

What does denaturation not change

A

Primary structure

253
Q

What is an optimum temperature

A

The temperature in which an enzymes rate of reaction is maximum

254
Q

What is the optimum temperature a balance of

A

Increasing kinetic energy and increasing vibration

255
Q

How can we measure the effect of temperature on enzyme action

A

Varying out an enzyme controlled reaction at different temperatures using a water bath.
To measure production of products or disappearance of substrate check 2.1.27 &28

256
Q

Example of when heat resistant enzymes are used

A

Polymerase chain reaction in catalysing reaction to make many copies of DNA segments

257
Q

What determines the enzymes optimum temperature

A

What type of environment organism lives in

Organisms internal temperature that can be maintained

258
Q

What is ph

A

A measure of the hydrogen ion (H+) concentration

259
Q

Concentration of h+ at a low pH

A

High

260
Q

Why is acid defined as a proton donir

A

Because hydrogen ions arw also known as protons

261
Q

How can hydrogen ions interference with the tertiary structure of an enzyme/active site

A

Cz of the charge of hydrogen ions and hydrogen and ionic bonds in the tertiary structure of an enzyme they can interfere with the tertiary structure thus function

262
Q

How can changes in pH affect enzyme

A

They interference with the bonds in the tertiary structure which leads to it changing which lead to it stopping from functioning which decreases reaction rate

263
Q

Hiw can change to active site cz of pH interfere induced fit hypothesis

A

Hydrogen ions will alter the charges around the active site cz they’re attracted to any negative charges around active site. This alter shape and means substrate can no longer fit

264
Q

What is optimum ph

A

The pH at which the rate of reaction is highest

265
Q

How does the best overall shape help in terms of hydrogen ions and optimum pH

A

Holds the active site in the shape that best fits the substrate

266
Q

Hiw do you measure effect of pH on enzyme action

A

Involves carrying out enzyme controlled reactions at different pH using buffer solution. To measure production of products or disappearance of substrate check 2.1.27 & 28

267
Q

Examples of enzymes operating at different pH leveks

A

Pepsin works in stomach with an optimu pH of 2 eg kills bacteria

Trypsin works in small intestine optimum pH is 7 neutralises food

268
Q

What I’d a buffer

A

A chemical solution that resist changes in pH by maintaining a constant level of hydrogen ions in the solution

269
Q

Difference between minor and major changes in pH in terms of denaturation

A

Minor changes don’t denature enzymes, bonds can be reformed

Major changes aren’t reversible, lead to denatured enzyme

270
Q

What happens if there’s no substrate

A

Reaction can’t proceed because enzyme substrate complexes can’t be formed

271
Q

What happens if concentration of substrate increase with a fix amount of enzymes

What if it increases even further

A

Collision occur more often
Enzyme substrate complexes increase
Products increase
Reaction rate increases

Reaction rate reaches maximum value

272
Q

What does it mean when a reaction rate reaches maximum level in terms of increasing substrate concentration

A

All the active sites are occupied

No effect if substrate concentration is increased

273
Q

What happens if you increase enzyme concentration with a fix amount of substrate concentration

What if you keep increasing it

A

More collision
More enzyme substrate complexes
More products at a given time
Increase in reaction rate

But eventually maximum reaction rate will be reached

274
Q

What happens at a maximum reaction rate in terms of increasing enzyme concentration

A

All the substrate molecules are used up and no other are free to bind with other active sites

275
Q

In an enzyme controlled reaction when is the reaction rate highest

A

When substrate and enzyme are mixed together

276
Q

What does the initial reaction rate do

A

Gives the maximum possible reaction rate for an enzyme under a particular experimental situation

277
Q

What is another word for leveling off in graphs

A

Plateau

278
Q

What is a limiting factor

A

A factor where if all other conditions are kept constant, increasing the concentration of that factor alone will increase the reaction rate

279
Q

What is control of metabolism based on

A

Control/regulation of enzyme activity

280
Q

How could you regulate enzyme activity

4 examples

A

PH concentration
Temperature concentration
Substrate concentration
Enzyme concentration

281
Q

what is an enzyme inhibitor

A

a substance or molecule that slows down the rate of an enzyme controlled reaction by affecting the enzyme molecule in some way

282
Q

what are the 3 types of inhibitors?

A

competitive and non-competitive and permanent

283
Q

talk about competitive inhibitors

A

similar shape to that of the substrate molecule
so they can occupy the active site
they form an enzyme-inhibitor complex
doesn’t lead to formation of products cz inhibitor isn’t identical to the substrate
the enzyme doesn’t catalyse a reaction

284
Q

what happens to reaction rate during enzyme inhibition and why

A

decrease

cz less enzyme-substarte complexes are being formed so less prodcts cz inhibitor is occupying the active site2

285
Q

what does the level of inhibition depend on in competetive inhibition?

A

level of inhibiotrs or substrate molecules. the more the substrate mlecules the more likely theyll collide with an active site

286
Q

talk about non-competitive inhibiotrs

A

dont compete with substrate molecules for the cative site because they dont bind with the active site
the attachment distorts the tertiary structure of the enzyme
this mean the active site shaoe changes
so the substrate no longer fit even though the inhiviotr isnt binded to the active site
which decreases amount of substrate-nzyme complexes which decreases reaction rate

287
Q

what does the level of inhibition depend on in non comp inhibition

A

amount of inhbitor molecules

substrate conc has no effect

288
Q

what are most comp inhibitors

what is their action described as

A

dont bind permanetnly

reversible

289
Q

what happens if an enzyme molecules is bound by a permanent inibitor?

A

denatured

290
Q

whys inhibition not always bad

A

cz it controls reaction rate by regulating metabolic pathways

291
Q

What are cofactors

A

Any substance that must be present to ensure enzyme controlled reactions take place at the appropriate rate

Some factors are a part of the enzyme (prosthetic groups) others affect an enzyme in a temporary basis (coenzymes and inorganic ion cofactors)

292
Q

Talk about coenzymes

A

Small, organic, non protein molecules that bind for a short period if time to the active site
Bind just before or at the same time the substrate binds
Like substrate they change in some way
Unlike substrates they are recycled back to take part in the reaction again
Role ills often to carry chemical groups between enzymes so they link together enzyme controlled reactions that need to take place in sequence

293
Q

Example of a coenzyme

A

Vitamin b3

Helps body break down carbohydrates and fat ti release energy

This vitamin is used to make a coenzyme that is required for the enzyme pyruvate dehydrogenase to function properly which catalysed one of the reactions in the sequence involved in respiration. Normal growth can’t proceed without it

294
Q

Talk about prosthetic groups

A

A coenzyme that is a permanent part of an enzyme

Also found in other protein molecules such as haemoglobin

Ar vital for the function, contribute to the final 3D shape and to other properties including its charges.

295
Q

Example of a prosthetic group

A

Zinc based carbonic prosthetic group in carbonic anhydrase

Enzyme involved in catalysing the combining of CO2 and he to produce carbonic acid. Important reaction that enables CO2 to be transported in blood.

296
Q

Talk about inorganic ion cofactors

A

In some enzyme controlled reactions the presence of some ions can increase the reaction rate
Ions may coming with either the substrate or the enzyme
The binding of the ion makes the enzyme substrate complex form more easily cz it affects the charge distribution and sometime the shape of the enzyme substrate complex

297
Q

Example of inorganic ion cofactors

A

Chloride ion

Help amylase catalyse the breakdown of starch to maltose

298
Q

What inhibits cell respiration

Why

A

Potassium cyanide

Cz it’s a non competitive inhibitor for a vital respiratory enzyme called cytochrome oxidase found in mitochondria

Inhibition of it decreases use of O2 so ATP can’t be made

The organism can only respire anaerobically which leads to build up of lactic acid

299
Q

Talk about enzymes and medicines

A

Protease inhibits inhibit the viral protease enzymes often as competitive inhibitors

300
Q

Talk about replacement enzymes and cystic fibrosis

A

Enzymes ate prescribed in tablet form to indvs with cystic fibrosis in order to overcome the problem of not having enzymes

301
Q

Talk about ethylene glycol poisoning

A

if taken into the body it’s broken down in the liver by the enzyme alcohol dehydrogenase

Product oxalic acid is extremely toxic

Treatment includes using the drug fomepizole, which is a strong inhibitor of alcohol dehydrogenase so reduces rate of production of oxalic acid

Ethanol cam also inhibit the same reaction but can lead to alcohol intoxication

302
Q

Talk about antibiotics and bacterial enzymes

A

Antibiotics can kill or inhibit the growth of microorganisms

Inhibit a bacterial enzyme that forms cross links in the bacterial cell wall so walls of growing bacteria are not made so bacterial reproduction is halted

303
Q

What dies snake venom contain inhibitor

A

Inhibitor of acetylcholinesterase, results in paralysis cz it’s involved in nerve transmission

Contains enzyme hyaluronidase which breaks down connective tissue and so helps toxins to penetrates tissues quickly

Also contain ATP ases which are used for breaking down ATP to disrupt the preys use of energy.

304
Q

What is the turnover number for an enzyme

A

The number of reactions an enzyme molecule can catalyse in one second

In catalase, the turnover number is up to 200k

305
Q

What are chains of enzyme reactions called

A

Metabolic pathways

306
Q

What are inborn errors of metabolism

A

Lack of functioning specific enzyme in a metabolic system

Biology Unit 2 (3 decks)

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