Polymers and Life(PL) Flashcards

1
Q

What is a polymer?

A

Long molecule made up from lots of small molecules called monomers

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2
Q

What is addition polymerisation?

A

When the monomer units need a double bond to be added

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3
Q

What is copolymerisation?

A

When more than one type of monomer is used in addition polymerisation

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4
Q

What are the two types of polymers and what is the difference between the two?

A
  • A-A polymers are made from all the same monomers
  • A-B polymers are alternating polymers, made from two monomers
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5
Q

Give an example of a co-polymer

A

Polyesters formed from a diol and carboxylic acid

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6
Q

What is copolymerisation?

A

When more than one type of monomer is used in addition polymerisation

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7
Q

Give three differences between addition and condensation polymerisation

A
  • Addition only one type of monomer is used/Condensation formed from two types of monomers
  • Addition formed from alkenes/Condensatioon formed from diols and carboxylic acids
  • Additions no other products other than the polymer/Condensation also produces a small molecule in addition to the polymer
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8
Q

What’s the sufix if a molecule has two carboxyl groups?

A

-dioic acid

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9
Q

What is formed from the reaction between an alcohol and a carboxylic acid?

A

An ester

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10
Q

What’s formed when carboxylic acids react with carbonates?

A

Salt + carbon dioxide + water

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11
Q

How do you name esters?

A

The group with C=O is the carboxylic acid and the group attached to the -o- id the alcohol

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12
Q

What is a base?

A

A molecule that accepts protons

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13
Q

How can amines be classified?

A

Primary,secondary and teriary based upon how mnay hydrogen atoms have been replaced by alkyl groups

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14
Q

When does the naming of amines switch order?

A

When the amino group is placed on a hydrocarbon chain with more than two carbons. The amino becomes the prefix

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15
Q

Three points

What are the properties of amines?

A
  • Amines can form hydrogen bonds with water
  • Amines with small alkyls are more soluble
  • Amines with larger alkyl groups less soluble as the enthalpy change to break hydrogen bond between water molecules is too great
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16
Q

What is the functional group of an amine?

A

NH2

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17
Q

How do amines act as bases?

A

When the lone electron pair on the nitrogen atom is donated, an amine acts as a H+ acceptor

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18
Q

What are amides and what is their functional group?

A

Amides are derivatives of carboxylic acids and their functional group is CONH2

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19
Q

What two functional groups is required to make a nylon or polyamide?

A

Diamines and dicarboxylic acids/acyl chlorides

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20
Q

What are acyl chlorides and why might we use them in place of carboxylic acids?

A

Acyl chlorides are reactive forms ofcarboxylic acids

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21
Q

What is formed when reacting an acyl chloride and an alcohol?

A

Esters

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22
Q

How are nylons named?

A

Nylon-x,y
x=numbe of carbon atoms in the diamine
y=number of carbon atoms in the dicarboxylic acids/diacyl chlorides

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23
Q

What are the products of esters in acid or alkanine hydrolysis?

A
  • Acid=carboxylic acid and alcohol
  • Alkanine=carboxylate salt and alcohol
24
Q

What are the products of a primary amide in acid hydrolysis and alkaline hydrolysis?

A
  • Acid=carboxylic acid and ammonium
  • Alkaline=carboxylate ion and ammonia
25
Q

What are the products of secondary amides in acid hydrolysis and alkaline hydrolysis?

A
  • Acid=carboxylic acid and ammonia+hydrocarbon chain
  • Alkaline=carboxylate ion and primary amide
26
Q

What’s the structure of an amino acid?

A

An amino group, carboxylic acid group, R group and the α-carbon

27
Q

What’s the α-carbon?

A

The first carbon attached to the carboxylic acid

28
Q

How do amino acids form zwitterions?

A

The hydrogen ion from the carboxylic acid group is donated to the amino group to from NH3

29
Q

What are bifunctional compounds and give an example

A

Bifunctional compounds are molecules with two functional groups e.g. amino acids

30
Q

Why are amino acids particualry soluble in water?

A

They are effectively ionic

31
Q

What are buffer solutions?

A

Solutions which cab withstand the addition of small amounts of acid or alkali

32
Q

Which bond is broken in the hydrolysis of amides?

A

C-N bond is broken by hydrolysis with either an acid or alkali catalyst

33
Q

Why does glycine not have optical isomerism?

A

There are only three different groups attached to the four bonds

34
Q

What is the definition of stereoisomerism?

A

Molecules have the SAME MOLECULAR FORMULA but the atoms are joined to each other in a DIFFERENT SPACIAL ARRANGEMENT - they occupy a different position in 3-dimensional space.

35
Q

What is the link formed between in two amino acids and what is its name?

A

The amino group and carboxylic acid group reacts to form a peptide link

36
Q

What are the three levels of protein structure?

A
  • Primary structure=the order of the amino acid residues
  • Secondary=the coiling parts of the chain folded into a helix or the formation of a region of sheet
  • Tertiary=the folding of the secondary sheet
37
Q

What is an enzyme?

A

A biological catalyst, this means it is produced in the body and increases the rate of reaction

38
Q

What are the four characteristics of an enzyme?

A
  • Highly specific
  • Sensative to tempature
  • Sensative to pH
  • Subject to competative inhibitors
39
Q

Why are enzymes highly specific?

A
  • They have a precise tertiary structure
  • A cleft in the enzyme (active site) due to how the protein folds, is tailored to fit a specific substrate molecules
40
Q

Why are enzymes sensative to pH?

A

Changing the pH changes ionisable groups
this can cause the tertiary structure to break, it is denatured

41
Q

Why are enzymes sensative to temperature?

A

Too much energy resulting in the intermolecular bonds, holding the tertiary structure, to breal

42
Q

What happens to the order of the substrate as the reaction progresses and why?

A

It goes from 1st order to 0 order
This is because the active site of the enzymes become fully saturated, preventing more of the substrate from binding

43
Q

How can inhibitors be used in everyday society?

A

Some medicine work by inhibiting the actioon of enzymes

44
Q

What is molecular recognition?

A

The ways in which molecules interact in terms of intermolecular and other non-covalent bonds

45
Q

What is a pharmacore?

A

The part of its molecule that gives the medicine its pharmological effect

46
Q

What are the characteristics of a pharmacore and how are they explained?

A
  • Can be modified by changing functional groups attached=can make medicine more effective and reduce side-effects
  • Interact with receptor sites by forming weak interactions
  • Fit into receptor with the correct size,shape and orientation=they can form correct weak bonds
47
Q

What information can be given by a proton n.m.r spectrum about a molecule?

A
  • How many different chemical environments there are
  • Ratios of the number of equivalent hydrogen atoms
  • Chemical environment of the non-equivalent hydrogen atoms
  • Number of adjacent hydrogen atoms that are non-equivalent
48
Q

Enzyme active site

How do inhibitors work in medicine?

A
  • Ihibitor has the same shape as the substrate
  • The inhibitor binds to the active site of the enzyme
  • This stops the substrate from binding to the active site of the enzymes
49
Q

Describe the structure of the monomer units in DNA

A
  • A phosphate group, deoxyribose sugar and a nirtogen containing base
  • Phosphodiester bonds bind the ribose sugar of one nucleotide to the phosphate group of another
  • Hydrogen bonds are found between complementry base pairs
50
Q

Not as detailed as biology (Four points)

Describe the process of transcription

A
  1. DNA molecules unzipped by DNA helicase
  2. Free nucleotides bind to the complementry bases~thymine is replaced with uracil
  3. Phosphodiester bonds are formed to create a sugar-phosphate backbone~for the mRNA template strand
  4. mRNA is formed and the DNA is re-formed
51
Q

Three points

Describe the process of transcription

A
  • Nucleotides in the mRNA are grouped together into codons~each codon corresponds to a specific amino acids
  • Each codon read by tRNA anti-codons and specific of amino acids are formed
  • Polypeptide chain formed ~then folds into secondary and tertiary structure for the protein
52
Q

What are two differences between RNA and DNA?

A

RNA=uracil and ribose sugar
DNA=thymine and deoxyribose sugar

53
Q

What do the number of peaks in NMR tell you?

A

The number of different carbon/hydrogen environments

54
Q

What type of resolution has splitting peaks?

A

High resolution NMR

55
Q

What does different types of spectra tell you about a molecule?

A
  • Low res NMR:Mr from M+ ion and fragments
  • High res NMR:molecular formula from the M+ ion
  • IR:certain fuctional groups
  • 13C NMR:the number and types of carbon environments
  • 1H NMR:number and types of hydrogen environments, number of hydrogen atoms in each environment and the number of adjacent hydrogen atoms