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
Q

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

A

diol and dicarboxylic acid

26
Q

what two functional groups does an amino acid have

A

NH2 and COOH

27
Q

what does the NH2 group act as in an amino acid

A

Base so it can accept H+

28
Q

what does the COOH group act as in an animo acid

A

acid so can donate H+

29
Q

when do zwitterions form

A

neutral Ph and in a solid state

30
Q

what is a zwitterion

A

amino acid with NH3+ group
and a COO:- group

31
Q

what happens to amino acids in acidic conditions

A

they get protonated

32
Q

what happens to amino acids in alkali conditions

A

they get deprotonated

33
Q

define a dipeptide

A

when two amino acids join together

34
Q

define a tripeptide

A

when 3 amino acids join together

35
Q

define a polypeptide

A

when more then 3 amino acids join togther

36
Q

what is an amide link also known as

A

polypeptide bond

37
Q

what kind of reaction occurs when 2 amino acids join together

A

condensation reaction as water is lost

38
Q

conditions for hydrolysising a peptide back to its constitue amino acids

A

boil for 24 hours
6 mol dm^-3 HCl catalyst

39
Q

describe a primary structure protein

A

straight line of amino acids

40
Q

describe a secondary structure protein

A

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
Q

name the 2 3D shapes that a secondary structure protein can have

A

alpha helix
beta pleated sheet

42
Q

describe how a tertiary structure is formed

A

alpha helix or beta pleated sheet folds into a 3D shape called a tertiary structure

43
Q

how are tertiary structures held in place

A

hydrogen bonds
some ionic interactions
disulphide bonds

44
Q

what is a disulphide bond also known as

A

S-S

45
Q

how can a disluphide bond be represented in an exam

A
46
Q

how many reactions can each enzyme catalyse

A

one type

47
Q

why are enzymes stereospecifc

A

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
Q

describe how drug development takes place (enzyme inhibition)

A

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
Q

describe how you would denature an enzyme

A

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