Biological Molecules Flashcards

A level - AQA

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1
Q

describe how a peptide bond is formed between two amino acids to form a dipeptide

A

condensation reaction between amine and carboxyl

peptide bond formed between c and N

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2
Q

how is the secondary structure of a polypeptide produced by bonds between amino acid

A

hydrogen bonds
between NH and C=O
forming a helix

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3
Q

two proteins have the same number and type of amino acids but different tertiary structure, explain why

A

different sequences of amino acids which cause different primary structures
this forms ionic/hydrogen/disulphide bonds in different places

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4
Q

compare and contrast the processes by which water and inorganic ions enter

A

comparison :
• both move down a concentration gradient
• both move throught protein channels in membrane
contrast :
• ions can move against a concentration gradient by active transport

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5
Q

how to test for lipids

A

dissolve in alcohol and then add water

white emulsion shows presence of lipid

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6
Q

describe the structure of glycogen

A

polysaccharide of α glucose

joined by glycosidic bonds with branched structure

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7
Q

how is glycogen used as a source for energy in animals

A

hydrolysed into glucose

glucose used in respiration

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8
Q

how is glycogen used as a source for energy in animals

A

hydrolysed into glucose

glucose used in respiration

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9
Q

difference between phospholipid and triglyceride

A

in phospholipid a fatty acid is replaced by a phosphate

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10
Q

difference between saturated and unsaturated fatty acids

A

saturated only has single bonds between carbon and unsaturated has single and double bonds between carbons

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11
Q

why wouldn’t a fat substitute be digested by lipase

A

Enzymes are specific, the fat substitute isnt complementary so is unable to bind to lipase

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12
Q

Give ways ATP is a suitable source for cells to use

A

NOTICE IN CONTEXT OF STORAGE

  1. releases relatively small amount of energy (small manageable bursts)
  2. releases energy instantaneously
  3. phosphorylates other compounds, making them more reactive
  4. can be rapidly synthesized
  5. is not lost from cells
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13
Q

does anaerobic reaction occur in organelles?

is electron transport chain involved?

A

no

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14
Q

does aerobic reaction and photosynthesis occur in organelles?
is electron transport chain involved?

A

yes

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15
Q

write a simple equation to show how ATP is synthesized from ADP

A

ADP + Pi -> ATP

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16
Q

Give two ways that the properties of ATP make it a suitable source of energy in biological processes

A

NOTICE tHAT THE qUESTION IS ASKING IN CONTEXT OF RELEASE NOT STORAGE

  1. Energy released in small suitable amounts
  2. Soluble
  3. involves a simple/single reaction
17
Q

why is it necessary for them tp synthesise such a large amount of ATP

A
  1. ATP can not be stored (bc its an immediate store of energy)
  2. ATP only releases a small amount of energy af a time
18
Q

why would you suspend a mitochondria in an isotopic solution

A

prevent damage to mitochondria caused by differences in water potential/osmosis/water

19
Q

when glucose is released what happens to energy not incorporated into ATP

A

released as heat

20
Q

when one mole of glucose is respired anaerobically, only 2 moles of ATP are produced,
explain why less energy is released

A

glucose is only partly broken down

only broken down to lactate

21
Q

at the end of a sprint race, a runner continues to breathe rapidly for some time, explain the advantage of this

A

lactis acid has been built up

oxygen used to break down lactic and convert it back to glucose

22
Q

name the substance that muscles use as their immediately energy source

A

ATP

23
Q

cats are lactose intolerant, lactase is used to hydrolyse lactose, making milk hydrolysis lactose free
why used lactase coated beads instead of direct lactase

A
1 beads are reusable
2 no need to remove lactase afterwords
3 allows continuous process 
4 enzyme is more stable 
5 avoid end product inhibition
24
Q

suggest why does lactose-free milk (galactose is hydrolysed) tastes sweeter after than the cows milk with lactose

A

lactose is hydrolysed to glucose and galactose so more sugar molecules present

25
Q

suggest why does lactose-free milk (galactose is hydrolysed) tastes sweeter after than the cows milk with lactose

A

lactose is hydrolysed to glucose and galactose so more sugar molecules present

26
Q

give two ways the structure of starch is similar to cellulose

A
1 are polymers 
2 contain glucose/carbon/hydrogen and oxygen
3 contain glycosidic bonds
4 have 1-4 links 
hydrogen bonding
27
Q

give two ways starch is different from cellulose

A

1 starch contains α glucose and cellulose contains β glucose
2 starch is branched and coiled while cellulose is unbranched and straight
3 starch also has 1-6 branching
4 starch doesn’t have hydrogen bonds berween moleculess
5 starch has glucose/monomers same way up
6 starch doesn’t have fibres

28
Q

explain difference between the structure of statch molecule and cellulose molecule

A

1 starch formed from α glucose but cellulose formed from β glucose
2 position of hydrogen and hydroxyl groups on carbon atom 1 inverted

29
Q

explain one way in which starch molecules are adapted for their function in plant cells

A
1 insoluble 
2 so dont affect water potential
or
1 helical
2 compact
or
1 large molecules 
2 can not leave cells
30
Q

explain how cellulose moelcules are adapted for their function in plants

A

long straight chains
become linked together by many hydrogen bonds to form fibrils
provide strength to cell wall

31
Q

when wheat ia hydrolysed what sugars would you sugar would you expect and why?

A

maltose

salivary amilase breaks down starch

32
Q

using the ides of water potential, explain why adults that can not digest lactose get diarrhoea when they drink milk

A

SOLUBLE lactose isnt hydrolysed
lowers water potential in the lumen
causing water to enter lumen by osmosis

33
Q

explain the difference of effect of chewing vs chopping on the digestion in wheat

A

some strach is already digested when chewing in mouth
faster digestion of chewed starch
same amount of digestion at the end of time

34
Q

describe competitive and non competitive inhibition of enzymes

A

1 inhibitors reduce binding of enzyme to substrate/prevent formation of enzyme substrate complex

2 competitive inhibition, inhibitor similar shape to substrate
3 binds in to active site
4 inhibition can be overcome by more substrate
5 non competitive inhibition, inhibitor binds to site on enzyme other than active site
6 changes shape of active site
7 cannot be overcome by adding more substrate

35
Q

explain how sports drinks could provide an energy boost when running

A

1 drink contains carbohydrates so raises blood glucose concentration quickly
2 contains salt so glucose more rapidly absorbed
3 increases glucose to muscles for respiration
4 faster energy release

36
Q

for enzyme related reactions how could you set up a control experiment?

A

boil the enzyme

37
Q

describe the structure of proteins

A

polymers of amino acids
joined by peptide bonds
formed by condensation
primary structure is sequence of amino acids
secondary structure is folding of polypeptide chain due to hydrogen bonding to form alpha sheet or beta pleated sheet
tertiary structure is 3D folding due to hydrogen bonding, ionic bonding and disulphide bonds
quarternary structure is two or more peptide chains

38
Q

describe how proteins are digested in the human gut

A

hydrolysis of peptide bonds
endopeptidaeses break polypeptides into smaller peptide chains
exopeptides remove terminal amino acids;
dipeptidaeses hydrolyse/break down dipeptides into amino acids

39
Q

what sugars do you expect to produce when chewing and why

A

maltose

salivary enzymes breaks down starch