polymers amino acids and DNA Flashcards

1
Q

what is a single strand of DNA made up of

A

4 diffrent monomers

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2
Q

what 3 things is a monomer/nucleotide made up of ?

A

a phosphate
a sugar
a base

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3
Q

adenine is bonded with ….. and forms …. hydrogen bonds

A

thymine
2

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4
Q

guanine is bonded with ….. and forms …. hydrogen bonds

A

cytosine
3

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5
Q

describe cell division

A

hydrogen bonds between base pairs break
2 strands start to unravel
new nucleotides come and attach to the standard strands
the new nucleotides polymerise together by forming a phosphate sugar bond
this creates a second complementary strand of DNA giving 2 full DNA molecules

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6
Q

considerations of using cis platin

A

also bonds to healthy cells
can cause unwanted side effects
targeted straight to the cells ro reduce the effect on healthy tissue
can also be used in minimal amounts

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7
Q

cis platin

A

PtCl2(NH3)2

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8
Q

define an addition polymer

A

long chain formed from many monomers and no other product is formed

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9
Q

define a condensation polymer

A

2 molecules join to form a larger one and a small molecule like H2O or HCl is realised

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10
Q

what is a polyester formed from

A

dicarboxycilic acid and a diol
or
diol and diacyl chloride

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11
Q

what is terylene formed from

A

ethane-1,2-diol
and
benzene-1,4-dicarboxylic acid

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12
Q

use of terylene

A

carpets clothing
heat treated polyesters used for drinks bottles

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13
Q

what are polymers containing amide links known as

A

polyamides of polypeptides

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14
Q

what two monomers make up polyamides

A

dicarboxylic acid and diamine
or
diamine and diacyl chloride

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15
Q

what is nylon6,6 made up of

A
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16
Q

draw 2 repeating units of nylon 6,6

A
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17
Q

what monomers make up kevlar

A
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18
Q

draw two repeating units of kevlar

A
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19
Q

name use and properties of nylon

A

used as fibres in clothing
as it’s elastic, strong abrasion resistant

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20
Q

use of kevlar and it’s properties

A

kevlar is used in the manufacturing of body armour and crash helmets
it’s strong light and heat resistant

21
Q

are addition polymers biodegradable?
why ?

A

no they aren’t
they have non polar C-C bonds that can’t be hydrolysed

22
Q

how are addition polymers disposed off

A

incinerated or buried
both of these have significant environmental issues

23
Q

are condensation polymers biodegradable
why ?

A

they are
as they can be hydrolysed in acidic or basic conditions
the delata positive C of the polar C-O bond can be attacked by nucleophiles

24
Q

what’s formed when you complete base hydrolysis on a polyester

A

Di-salt and diol

25
what’s formed when you complete acid hydrolysis on a polyester
diol and dicarboxylic acid
26
what two functional groups does an amino acid have
NH2 and COOH
27
what does the NH2 group act as in an amino acid
Base so it can accept H+
28
what does the COOH group act as in an animo acid
acid so can donate H+
29
when do zwitterions form
neutral Ph and in a solid state
30
what is a zwitterion
amino acid with NH3+ group and a COO:- group
31
what happens to amino acids in acidic conditions
they get protonated
32
what happens to amino acids in alkali conditions
they get deprotonated
33
define a dipeptide
when two amino acids join together
34
define a tripeptide
when 3 amino acids join together
35
define a polypeptide
when more then 3 amino acids join togther
36
what is an amide link also known as
polypeptide bond
37
what kind of reaction occurs when 2 amino acids join together
condensation reaction as water is lost
38
conditions for hydrolysising a peptide back to its constitue amino acids
boil for 24 hours 6 mol dm^-3 HCl catalyst
39
describe a primary structure protein
straight line of amino acids
40
describe a secondary structure protein
3D shape hydrogen bonds form between 2 peptide chains electron deficient H from NH attracts the lone pair on the O from C=O
41
name the 2 3D shapes that a secondary structure protein can have
alpha helix beta pleated sheet
42
describe how a tertiary structure is formed
alpha helix or beta pleated sheet folds into a 3D shape called a tertiary structure
43
how are tertiary structures held in place
hydrogen bonds some ionic interactions disulphide bonds
44
what is a disulphide bond also known as
S-S
45
how can a disluphide bond be represented in an exam
46
how many reactions can each enzyme catalyse
one type
47
why are enzymes stereospecifc
the shape of an enzymes active site is so specific to the substrate that in many cases one optical isomer will fit but another optical isomer may not
48
describe how drug development takes place (enzyme inhibition)
1) an undesirable biological process occurs which is catalysed by an enzyme 2) a computer is used to determine the shape of the active site and design another molecule which will fit into the active site. this must be the correct enantiomer 3) the new molecule is called the inhibitor. this fits into the active site and prevents the substrate from reacting in the active site
49
describe how you would denature an enzyme
heating it up if changing the ph will break the intermolecular forces holding the tertiary and secondary structure in place this will change the shape of the enzyme and it’s active site this in turn will stop the reaction being catalysed