Polymers, Amino Acids & DNA Flashcards

1
Q

What is a polymer

A

A long chain molecule formed from thousands of small molecules called monomers

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2
Q

What are the 2 types of polymer

A

Addition

Condensation

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3
Q

What happens during addition polymerisation

A

Unsaturated molecules (alkenes) add together

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4
Q

How are condensation polymers formed

A

By a condensation reaction where a small molecule like water is released

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5
Q

What are 2 examples of condensation polymers

A

Polyamides

Polyesters

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6
Q

What are 2 ways condensation polymers are formed

A

2 moments with functional groups at both ends of the molecule

One monomer such as amino acid with 2 functional groups on the molecule

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7
Q

How are polyesters formed from 2 monomers and 1 monomer

A

Do carboxylic acid and a diol

One monomer with both the carboxylic acid and the alcohol group

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8
Q

Where is the H and OH lost from when drawing repeating units of polyesters

A

OH from the carboxylic acid
H from the alcohol group

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9
Q

What is the ester link

A

C double bond O and O

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10
Q

How many molecules of water are lost when polyesters are made

A

(2n-1)

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11
Q

What 2 monomers are reacted to form polyamides

What monomer is used to form polyamides

A

Dicarbixylic acid and a diamine

Or react amino acids which have both groups

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12
Q

What is the H and OH lost from when drawing polyamide repeat units

A

OH from carboxylic acid
H from amine

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13
Q

Draw an amide link

A

Photo

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14
Q

What 2 monomers make terylene

A

Benzene 1,4 dioic acid
Ethane 1,2 diol

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15
Q

How many water molecules are lost when polyamides are formed

A

(N-1)

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16
Q

How is Kevlar made

A

Benzene 1,4 dioic acid
Benzene 1,4 diamine

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17
Q

What is a property and use of Kevlar

A

Incredibly tough
Bulletproof jackets

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18
Q

What 2 monomers are used to make nylon6,6

A

Hexanedioic acid
Hexane 1,6 diamine

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19
Q

What are polyesters used to make

A

Fibres and plastic bottles for fizzy drinks

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20
Q

Why is pet the main plastic for making fizzy drink bottles (3)

A

It’s light, strong and resistant to corrosion

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21
Q

What is hydrogen bonding in polyamides

A

The lone pair on oxygen in the C double bond O forms a hydrogen bond with the delta positive bridges in the NH of another chain

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22
Q

Where do permanent dipole dipole forces exist in polymers

A

In polyesters and addition polymers that have electronegative atoms as functional groups

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23
Q

In acid hydrolysis of polyesters what is formed

What type of reaction is it

A

The carboxylic acid and the diol

Reversible

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24
Q

In base hydrolysis of polyesters what is formed

A

The salt of the carboxylic acid and the diol

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25
Q

How do you get the carboxylic acid back in de hydrolysis of polyesters

A

By neutralising the salt

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26
Q

What is formed in the acid hydrolysis of polyamides

What type of reaction is it

A

The carboxylic acid
The di ammonium ion (pronated diamine)

Reversible reaction

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27
Q

What is formed in the base hydrolysis of polyamides

A

The salt of the carboxylic acid and the diamine

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28
Q

Why is base hydrolysis the preferred method

A

It’s not a reversible reaction so 100% yield can be achieved
Whereas acid hydrolysis is reversible so it has a lower yield

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29
Q

What are 3 ways of disposing of polymers

A

Landfill
Recycling
Burning / incineration

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30
Q

What is 2 advantages of recycling

A

It reduces the amount of plastic disposed in landfill sites

It conserves crude oil which is the source of most monomers used

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31
Q

What is a disadvantage of recycling

A

The plastics must be collected, sorted and processed which is expensive

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32
Q

Why are addition polymers chemically unreactive

A

They are saturated compounds and don’t have polar bonds

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33
Q

What is an advantage of addition polymers being non polar
What is a disadvantage

A

They are useful as they aren’t attacked by acids, bases or oxidising agents

It makes them non biodegradable

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34
Q

Why are polyalaknes not bio degradable (3)

A

They are inert
They have polar bonds
Not easily attacked by nucleophiles

35
Q

Why are condensation polymers biodegradable (2)

A

They gave polar bonds

Can be hydrolysed by Nucleophiles

36
Q

Draw the general structure of amino acids

A

Photo

37
Q

Why do amino acids exhibit both basic and acidic properties

A

They have both a carboxylic acid and an amine group

38
Q

How is the NH2 group in amino acids basic

A

It can gain a H+ ion to form NH3+

39
Q

Why is the COOh group acidic

A

It cha lose a H+ to form COO- ion

40
Q

How do amino acids act as acids and as bases

A

They donate protons to bases

As bases they accept protons from acids

41
Q

What is the structure of glycine

A

Photo

42
Q

What are amino acids like in their pure state (3)

A

White crystalline solids with a relatively high melting point for their mr

Generally soluble in water to produce a solution that conducts electricity

Most insoluble in non polar solvents

43
Q

Why do amino acids have high melting points

A

They have ionic bonding in their solid form as they exist as zwitteriojs in their pure state

44
Q

What is a zwitterion

A

A diplomat in with both a positive and negative change on different parts of the molecule

45
Q

What is the isoelectric point

A

The ph at which the overall charge on an amino acid is 0

46
Q

What happens when the ph is decreased in amino acids in their pure state (zwitterions)

A

The COO- group gains a proton

47
Q

What happens when the ph is increased in amino acids in their pure state

A

The NH3+ group loses a proton

48
Q

What is the most important reaction of amino acids and how does it occurs

A

Polymerisation
Occurs by condensation reactions

49
Q

How are peptides and proteins formed

A

The enzymes catalyse the polymerisation of amino acids in living organism

50
Q

How is a tripeptide formed

A

From 3 amino acids

51
Q

How are polypeptides formed (2)

A

From joining many amino acids

Or linking 2 peptide chains together

52
Q

What are the conditions for hydrolysing proteins

A

Boiling the protein with 6mol dm-3
HCL for 24 hours

53
Q

Why do amino acids have different RF values

A

They have different r groups so they have different solubilities in the mobile phase

54
Q

What chemical makes amino acids visible in tlc

A

Ninhydrin

55
Q

What is the primary structure in proteins

A

The order or sequence of amino acids in the protein chain

56
Q

What is the secondary structure id proteins

A

The hydrogen bond interaction between amino acids within the same chain causing the chain to have areas of 3D sections

57
Q

What do the secondary structures of amino acids consist of (2)

A

Alpha helix

And beta pleated sheets

58
Q

What is the tertiary structure of proteins and why does this occur

A

The way in which the protein helix is bent, twisted or folded

The interactions between R groups in the amino acids that make up the protein

59
Q

What are the possible interactions between R groups in amino acids

A

Hydrogen bonding
Ionic bonding
Dipole dipole interactions
S-S bonds

60
Q

When do hydrophobic interactions occur

A

Between non polar side chains in tertiary structures

61
Q

When do disulfide bonds occur

A

Between 2 amino cysteine amino acids in tertiary structures

62
Q

What type of reaction is a disulfide bond formation

A

Oxidation (loss of hydrogen )

63
Q

What are all enzymes

A

Proteins

64
Q

What part of the enzymes is involved in catalysis
What is the rest if the amino acids for

A

The active site

Maintaining the precise shape of the enzyme and active site

65
Q

What is stereospecific

A

The active sites of enzymes only bind / react with one particular stereoisomer (ez or optical)

66
Q

What do active sites of enzymes do

A

They bind the substrate molecules of a biochemical reaction

67
Q

Why is it important to maintain the specific physical and chemical requirements of enzymes

A

Changes in physical (temp) or chemical (ph) factors can break the secondary and tertiary structures which changes the active site and affects catalytic activity

68
Q

What are enzymes inhibitors

A

Molecules that have similar shapes to the active site and compete with the reactant molecules (substrates) to bond to the active site

69
Q

What happens when enzyme inhibitors block active sites

A

They prevent catalysis from happening as the reactant molecules can’t fit into the active sites anymore

70
Q

What does the amount of inhibition depend on (3)

A

The relative concentrations of reactant (substrate) and inhibitors

The more inhibits the more active sites blocked

Also depends how strongly the inhibitor bonds to the active site

71
Q

How can enzyme inhibition be useful

A

It is used in some antibiotics to block the active sites of an enzyme in bacteria which makes cell walls
This causes the cell walls to weaken and over time the bacteria bursts

72
Q

How are enzyme inhibitors developed

A

Computers are used to model the shape of the enzyme active site and predict how well potential drugs will bind with the active site

73
Q

What are nucleotides

A

Nitrogen containing organic substances that form the basis of the nucleic acids dna and rna

74
Q

What 3 groups do all nucleotides contain

A

Phosphate group (circle )
Nitrogen containing base (hexagon)
Penrose sugar (pentagon )

75
Q

What is the sugar in dna

A

2 depxyribose

76
Q

What forms the basis of the nucleic acid DNA

A

Polynucleotides which are formed by nucleotides polymerising

77
Q

How are 2 DNA nucleotides joined

What type of reaction is it

A

When the OH group on C3 joins to the phosphate group on C5 to form a phosphodiester bond

Condensation

78
Q

What are the complimentary pairs in DNA

How are they linked

A

AT and CG

Hydrogen bonds

79
Q

How many hydrogen bonds are C and G linked by

A

3

80
Q

How many hydrogen bonds are A and T linked by

A

2

81
Q

How does cis platin work

A

It prevents dna replication by preventing the DNA double helix molecule from unwinding

It does this by forming co ordinate bonds with the nitrogen in the dna base guanine

82
Q

What are 3 risk of using cis platin

A

Prevents normal cells form replicating too (hair loss)

Patients experience side effects like nausea and kidney damage

Patients can become resistant to cis platin

83
Q

What are 2 reasons cis platin is still used despite the side effects

A

The benefits outweigh the side effects

Doctors use small amounts to reduce the side effects