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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
How do you get the carboxylic acid back in de hydrolysis of polyesters
By neutralising the salt
26
What is formed in the acid hydrolysis of polyamides What type of reaction is it
The carboxylic acid The di ammonium ion (pronated diamine) Reversible reaction
27
What is formed in the base hydrolysis of polyamides
The salt of the carboxylic acid and the diamine
28
Why is base hydrolysis the preferred method
It’s not a reversible reaction so 100% yield can be achieved Whereas acid hydrolysis is reversible so it has a lower yield
29
What are 3 ways of disposing of polymers
Landfill Recycling Burning / incineration
30
What is 2 advantages of recycling
It reduces the amount of plastic disposed in landfill sites It conserves crude oil which is the source of most monomers used
31
What is a disadvantage of recycling
The plastics must be collected, sorted and processed which is expensive
32
Why are addition polymers chemically unreactive
They are saturated compounds and don’t have polar bonds
33
What is an advantage of addition polymers being non polar What is a disadvantage
They are useful as they aren’t attacked by acids, bases or oxidising agents It makes them non biodegradable
34
Why are polyalaknes not bio degradable (3)
They are inert They have polar bonds Not easily attacked by nucleophiles
35
Why are condensation polymers biodegradable (2)
They gave polar bonds Can be hydrolysed by Nucleophiles
36
Draw the general structure of amino acids
Photo
37
Why do amino acids exhibit both basic and acidic properties
They have both a carboxylic acid and an amine group
38
How is the NH2 group in amino acids basic
It can gain a H+ ion to form NH3+
39
Why is the COOh group acidic
It cha lose a H+ to form COO- ion
40
How do amino acids act as acids and as bases
They donate protons to bases As bases they accept protons from acids
41
What is the structure of glycine
Photo
42
What are amino acids like in their pure state (3)
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
Why do amino acids have high melting points
They have ionic bonding in their solid form as they exist as zwitteriojs in their pure state
44
What is a zwitterion
A diplomat in with both a positive and negative change on different parts of the molecule
45
What is the isoelectric point
The ph at which the overall charge on an amino acid is 0
46
What happens when the ph is decreased in amino acids in their pure state (zwitterions)
The COO- group gains a proton
47
What happens when the ph is increased in amino acids in their pure state
The NH3+ group loses a proton
48
What is the most important reaction of amino acids and how does it occurs
Polymerisation Occurs by condensation reactions
49
How are peptides and proteins formed
The enzymes catalyse the polymerisation of amino acids in living organism
50
How is a tripeptide formed
From 3 amino acids
51
How are polypeptides formed (2)
From joining many amino acids Or linking 2 peptide chains together
52
What are the conditions for hydrolysing proteins
Boiling the protein with 6mol dm-3 HCL for 24 hours
53
Why do amino acids have different RF values
They have different r groups so they have different solubilities in the mobile phase
54
What chemical makes amino acids visible in tlc
Ninhydrin
55
What is the primary structure in proteins
The order or sequence of amino acids in the protein chain
56
What is the secondary structure id proteins
The hydrogen bond interaction between amino acids within the same chain causing the chain to have areas of 3D sections
57
What do the secondary structures of amino acids consist of (2)
Alpha helix And beta pleated sheets
58
What is the tertiary structure of proteins and why does this occur
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
What are the possible interactions between R groups in amino acids
Hydrogen bonding Ionic bonding Dipole dipole interactions S-S bonds
60
When do hydrophobic interactions occur
Between non polar side chains in tertiary structures
61
When do disulfide bonds occur
Between 2 amino cysteine amino acids in tertiary structures
62
What type of reaction is a disulfide bond formation
Oxidation (loss of hydrogen )
63
What are all enzymes
Proteins
64
What part of the enzymes is involved in catalysis What is the rest if the amino acids for
The active site Maintaining the precise shape of the enzyme and active site
65
What is stereospecific
The active sites of enzymes only bind / react with one particular stereoisomer (ez or optical)
66
What do active sites of enzymes do
They bind the substrate molecules of a biochemical reaction
67
Why is it important to maintain the specific physical and chemical requirements of enzymes
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
What are enzymes inhibitors
Molecules that have similar shapes to the active site and compete with the reactant molecules (substrates) to bond to the active site
69
What happens when enzyme inhibitors block active sites
They prevent catalysis from happening as the reactant molecules can’t fit into the active sites anymore
70
What does the amount of inhibition depend on (3)
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
How can enzyme inhibition be useful
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
How are enzyme inhibitors developed
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
What are nucleotides
Nitrogen containing organic substances that form the basis of the nucleic acids dna and rna
74
What 3 groups do all nucleotides contain
Phosphate group (circle ) Nitrogen containing base (hexagon) Penrose sugar (pentagon )
75
What is the sugar in dna
2 depxyribose
76
What forms the basis of the nucleic acid DNA
Polynucleotides which are formed by nucleotides polymerising
77
How are 2 DNA nucleotides joined What type of reaction is it
When the OH group on C3 joins to the phosphate group on C5 to form a phosphodiester bond Condensation
78
What are the complimentary pairs in DNA How are they linked
AT and CG Hydrogen bonds
79
How many hydrogen bonds are C and G linked by
3
80
How many hydrogen bonds are A and T linked by
2
81
How does cis platin work
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
What are 3 risk of using cis platin
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
What are 2 reasons cis platin is still used despite the side effects
The benefits outweigh the side effects Doctors use small amounts to reduce the side effects

Chemistry (23 decks)

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