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chemistry > polymers and life > Flashcards

polymers and life Flashcards

1
Q

what is a polymer

A

a polymer is a large molecule made with repeating units called monomers

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2
Q

what are the two types of polymer

A

addition polymer and condensation polymer

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3
Q

carboxylic acid functional group

A

COOH

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4
Q

what atoms are the partial charges of a carboxylic acid on

A

partially negative charge on oxygen, partially positive charge on carbon (of COOH group)

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5
Q

naming carboxylic acids

A

parent alkane + replace the “e” with “-oic acid”

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6
Q

general formula of carboxylic acids

A

Cn H2n+1 COOH

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7
Q

carboxylic acid solubility

A

carboxylic acids are soluble in water due to hydrogen bonding between the partially positive H and partially negative O in the COOH group and a water molecule

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8
Q

carboxylic acid solubility trends

A

as carboxylic acids get longer, solubility decreases

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9
Q

carboxylic acid acidic properties

A

carboxylic acids are weak acids, but the strongest organic acids

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10
Q

test for carboxylic acids

A

use sodium carbonate Na2CO3
carboxylic acid + sodium carbonate –> salt + water + carbon dioxide

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11
Q

carboxylic acid reaction with metal

A

–> salt + hydrogen

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12
Q

carboxylic acid reaction with base

A

–> salt + water

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13
Q

weak acid definition

A

acids that only partially ionise in solution (in a reversible reaction)

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14
Q

examples of carbonyl compounds

A

carbonyl compounds are ketones + aldehydes only

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15
Q

functional groups of an amino acid

A

carboxyl (COOH) and amino (NH2)

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16
Q

structure of an amino acid

A

HOOC - CRH - NH2

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17
Q

features of an amino acid

A

amphoteric - meaning have acidic and basic properties
sometimes exist as zwitterions

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18
Q

what are zwitterions

A

a molecule with both positive and negative ions, only exist at amino acid isoelectric point

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19
Q

amino acid at a low pH

A

COO- is likely to accept an H+ ion
HOOC-CRH-NH3+ structure

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20
Q

amino acid at a high pH

A

NH3+ group is likey to lose a H+ ion
-OOC-CRH-NH2

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21
Q

what are proteins

A

condensation polymers formed from amino acid monomers

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22
Q

bond between amino acid in a protein

A

peptide bond
-NH-C=O -

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23
Q

naming multiple amino acid molecules (proteins)

A

name starting from exposed NH2 group, then going along chain
use first three letters of amino acids, first letter is capitalised

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24
Q

structure + bonding of primary protein

A

the order of amino acids that form a protein chain
peptide bonds (covalent) between amino acids

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25
Q

structure and bonding of a secondary protein

A

primary structure folds due to hydrogen bonding between amino acids, forming either an alpha helix or a beta pleated sheet
hydrogen bonding between amino acid chains

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26
Q

structure and bonding of a tertiary structure protein

A

3D folding structure pattern due to R group interactions and folding of secondary structure
has hydrogen bonds, id-id bonds, ionic bonds, and covalent bonds (disulphide bridges) across polypeptide back bone

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27
Q

what is DNA

A

deoxyribonucleic acid
a polymer made up of nucleotide monomers

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28
Q

DNA nucleotide structure

A

a phosphate group, a pentose sugar (deoxyribose) and a nitrogenous base

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29
Q

nitrogenous base pairings in DNA

A

adenine bond with thymine with two hydrogen bonds
cytosine bonds with guanine with three hydrogen bonds

30
Q

what is RNA

A

ribonucleic acid
a polymer made up of nucleotide monomers

31
Q

RNA nucleotide structure

A

a phosphate group, a pentose sugar (ribose), and a nitrogenous base

32
Q

nitrogenous base pairings of RNA

A

adenine bonds to uracil with two hydrogen bonds
cytosine bonds to guanine with three hydrogen bonds

33
Q

formation of sugar-phosphate backbone in DNA

A

formed via condensation polymerisation between nucleotides, forming a phosphodiester bond between the phosphate group on one nucleotide and the sugar group on another nucleotide (loss of OH from phosphate group and H from sugar)

34
Q

why does complementary base pairing in DNA/RNA occur

A

adenine can only bond with thymine/uracil and cytosine can only bond with guanine because any other pairing would have two repelling partial charges close together, so they wouldn’t bond

35
Q

what are genes

A

a section of DNA that codes for a protein to be synthesised

36
Q

coding of amino acids

A

each amino acid is coded for by three bases, aka base triplets (DNA) or codons (RNA)

37
Q

basics of protein synthesis

A

DNA codes for specific amino acid sequences to form proteins
1. transcription
2. translation

38
Q

process of transcription

A
  1. DNA unwinds to reveal 2 separated strands
    2, free moving RNA bases are attracted to DNA bases
  2. RNA nucleotides are joined with the help of RNA polymerase enzyme
  3. DNA strands rejoin to form the double helix unchanged
  4. mRNA is free to move around and leaves the nucleus into the cytoplasm
39
Q

translation process

A

mechanism of joining amino acids to form polypeptide chains
1. when the ribosome reaches a start RNA codon it will not move until a tRNA with the correct anticodon base pairs match up with the mRNA bases
2. tRNA will be attached to a specific amino acid
3. ribosome will now move to next 3 mRNA bases repeating tRNA process, until a stop codon of mRNA is reached

40
Q

pharmacore meaning

A

the part of a drug molecule which fits into the cell receptor

41
Q

characteristics of enzymes

A
  • speed up reactions (biological catalysts)
  • sensitive to pH and temperature (become denatured if ideal enzyme environment is not met
  • active site is highly specific to a complementary substrate
  • similar molecules to the substrate can competetively inhibit enzyme activity by fitting in the active site
42
Q

enzyme reaction mechansim

A

E + S -> ES
ES -> EP
EP -> E + P
overall: E + S -> E + P

43
Q

rate determining step when reaction is first order w.r.t. substrate

A

E + S -> ES

44
Q

rate determining step when reaction is zero order w.r.t. substrate

A

EP -> E + P

45
Q

pH affect on enzyme

A
  • ionic groups in the active site are sensitive to pH change
  • high or low pH can cause the enzyme to become denatured
46
Q

temperature affect on enzyme

A
  • initially, there’s an exponential increase with more temperature, as more particles have energy greater than the activation energy
  • past optimum temperature weakens bonds (dipole-dipole or hydrogen bonds) in the tertiary structure are broken, denaturing the enzyme
47
Q

competitive inhibitors effect on enzymes

A
  • active site shows specificity
  • tertiary structure of enzymes only allows a particular molecule to enter its active site (molecular recognition)
  • even isomers can be determined using enzymes
  • competitive inhibitors have a similar structure to substrate so binds with complementary active site blocking E-S complex formation
48
Q

carboxylic acid reaction with metal carbonate

A

–> salt + carbon dioxide + water

49
Q

dipolar meaning

A

molecule with positive and negative charge (e.g. zwitterions)

50
Q

acyl chloride functional group

A

-C=O
Cl

51
Q

acid anhydride functional group

A

R-C=O O C=O - R

52
Q

ester functional group

A

R-COO-R

53
Q

aldehyde functional group

A

R-C=OH

54
Q

ketone functional group

A

R - C=O - R

55
Q

primary amine functional group

A

R-NH2

56
Q

secondary amine functional group

A

R2-NH

57
Q

hydrolysis of esters in acidic conditions

A

–> carboxylic acid + alcohol
conditions: heat and aqueous acid

58
Q

hydrolysis of esters in alkaline conditions

A

–> carboxylate salt + alcohol
conditions: heat and aqueous alkali

59
Q

hydrolysis of amides in acidic conditions

A

–> carboxylic acid + ammonium ion
conditions: heat under reflux

60
Q

hydrolysis of amides in alkaline conditions

A

–> carboxylate ion + ammonia
conditions: heat under reflux

61
Q

acyl chloride + alcohol

A

–> ester

62
Q

acyl chloride + ammonia

A

–> amide

63
Q

acyl chloride + amines

A

–> N-substituted amide

64
Q

amine solubility

A
  • soluble in water because the lone pair on the nitrogen forms hydrogen bonds with the water
  • Longer-chain amines are less soluble in water because the long chain needs to force itself between water molecules which are hydrogen bonded together; the enthalpy to break the water hydrogen bonds exceeds the enthalpy of formation of the new hydrogen bonds
65
Q

amide functional group

A

-CONH2
like a carboxylic acid COOH except the OH is replaced with an NH2

66
Q

testing for an acyl chloride

A

+ alcohol
If damp blue litmus paper is turned red by the released HCl, it’s an acyl chloride

67
Q

features of condensation polymers

A
  • monomers will be bifunctional (2 functional groups on the same molecule)
  • loss of a water molecule in polymerisation
  • the repeat unit is [two monomers drawn together]n
68
Q

features of an addition polymer

A
  • monomers are alkenes
  • addition reaction, involving the C=C double bonds of monomers breaking
69
Q

what is optical isomerism

A

when molecules have the same formula, but different arrangements so they are mirror images of each other (non-superimposable)

70
Q

criteria for optical isomerism

A
  • have four different groups around the chiral carbon (the central C atom)
71
Q

another name for optical isomers

A

enantiomers

72
Q

paper chromatography steps

A
  1. Draw a pencil line about 1cm from the bottom of the paper. Spot on the sample and reference samples onto this line (e.g. pure amino acid samples if detecting the compounds making up a polypeptide/protein)
    2) Suspend the plate in a beaker containing the solvent. Cover the beaker with a watch glass to saturate the air inside with the solvent
    3) Once the solvent reaches the top, remove the paper and let it dry
    4) Spots can be located with iodine, ninhydrin or UV. Now Rfs (the distance travelled by the spot divided by the distance moved by the solvent) can be calculated and analysed

chemistry (10 decks)

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