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human biology > module 1 -biological molecules > Flashcards

module 1 -biological molecules Flashcards

1
Q

what are biological molecules?

A

they are molecules that are made and used by living organisms eg proteins,lipids,DNA

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2
Q

what are monosaccharides?

A

they are the building blocks for carbohydrates, they cannot be hydrolysed into smaller carbs as they re the simplest form of them

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2
Q

what are the functions of carbohydrates?

A

they are used as an energy source( glucose in respiration)
as an energy store ( glycogen in animals)
and they can also be used for structure in plant cell walls.

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3
Q

give an example of monosaccharides?

A

glucose (alpha and beta)

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4
Q

what is the formula for monosaccharides?

A

the formula is C^6 H^12 O^6

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5
Q

what is the difference between alpha and beta glucose?

A

in the structure, they differ in position of their -OH groups on carbon 1

  • alpha glucose has a OH group on the bottom and beta glucose has it on the top ( above the ring)
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6
Q

how are monosaccharides joined together?

A

with a condensation reaction ( removing water )

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7
Q

what are 3 properties that monosaccharides have?

A

they are soluble in water
they form crystals
they taste sweet

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8
Q

how are disaccharides formed?

A

when 2 monosaccharides bond together during a condensation reaction.

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9
Q

give an example of a disaccharides?

A

glucose + glucose = maltose

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10
Q

what is the formula for disaccharides?

A

C^12H^22O^11

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11
Q

how are polymers seperated?

A

through hydrolysis, this is the chemical breakdown of a compound due to a reaction with water.

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12
Q

what is a polysaccharide?

A

they are just carbohydrates made up of many monosaccharides joined together by condensation reactions

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13
Q

name 3 important polysaccharides?

A

starch
glycogen
cellulose

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14
Q

what is structure of glycogen?

A

straight chain of alpha glucose with side branches

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15
Q

what are the properties of starch and glycogen?

A

-they are insoluble, do not affect water potential of the cell
-coiled so they can fit more into a cell and this is ideal for energy storage.
-they are branched, which helps with stored glucose being released very quickly.

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16
Q

where can glycogen be stored?

A

in the liver or the skeletal muscles

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17
Q

what is glycogenolysis?

A

it is the breakdown of glycogen.

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18
Q

what is the test for starch?

A

add iodine to the thing you are testing, if it turns blue or black it contains starch

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19
Q

what is the test for reducing sugar?

A

benedict’s test, use benedict’s reagent on heating for a few minutes, if it turns brick red/brown a reducing sugar is present.

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20
Q

what is the test for non reducing sugar?

A

heat with benedict’s, there will then be no change, so then you add dilute hydrochloric acid and then also add sodium Hydrocarbonate to neutralise this. heat this test sample again and it should tern a brick red.

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21
Q

what are 2 types of proteins?

A

globular and fibrous

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22
Q

what are globular proteins?

A

soluble proteins with a specific 3D shape eg enzymes, hormones

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23
Q

what are fibrous proteins?

A

strong/insoluble/inflexible material eg collagen

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24
Q

what are the building blocks for proteins?

A

amino acids

25
Q

what is the structure of amino acids? ( basic structure)

A

at the centre each amino acid is a carbon, then there is a carboxyl group to the right (COOH) , amine group to the left (NH2) , hydrogen above and R group below.

26
Q

what is the only unique feature in different amino acids? give an example of this

A

the R group
eg - glycine has a hydrogen in its R group

27
Q

how are amino acids joined together?

A

by a condensation reaction between the carboxyl group (COOH) of one amino acid and the amine group (NH2) of another
- this leaves a peptide bond from the carbon and nitrogen

28
Q

define primary structure?

A

it is the simplest level of protein structure, it has a unique sequence of amino acids, polypeptide chain that is held by a peptide bond.

29
Q

define secondary structure

A

the primary structure coils up to form an alpha helix, or also known as pleated sheets this is then held by hydrogen bonds

30
Q

define tertiary structure?

A

the secondary structure folds again to form the final 3D shape, this is held together by a number of different bonds and interactions between the R groups. eg hydrogen bonds, ionic bonds

31
Q

define quaternary structure

A

this is when proteins are made from more than one poly peptide chain

32
Q

what is a prosthetic group?

A

it is a non protein part of the protein structure and is needed for the functioning of the protein.

33
Q

give an example of a protein with a quaternary structure and a prosthetic group ?

A

haemoglobin

34
Q

describe the structure of collagen?

A

it is a strong material, used to build tendons and ligaments
primary structure is made up out of glycine( which is the simplest amino acid)
secondary structure forms a tight coil
tertiary structure then coils again
quaternary structure is made from 3 tertiary structures.
resulting in a collagen molecule

35
Q

what is the test for protein?

A

add biuret solution to the food being tested and mix that carefully, if this then turns into a purple colour then protein has been detected

36
Q

what is an enzyme?

A

a biological catalyst, that speeds up rate of reactions that does not get used up

37
Q

what is the induced fit model?

A

it is similar to the lock and key model but the active sight changes shape, so the substrate fits exactly to form an enzyme substrate complex

37
Q

what makes an enzyme specific?

A

they have a specific active site shape, only substrates that are complimentary to this shape can bind to this

38
Q

what is the effect of temperature on enzyme activity?

A

as temp increases, kinetic energy does too, molecules move faster, more successful collisions, increased rate of reaction and this carries out until the optimum is reached.

39
Q

however what happens if temperature rises above the optimum?

A

the bonds in tertiary structure start to break down, the active sight loses its shape, and enzyme substrate complexes can no longer be formed, causing the enzyme to denature

40
Q

what are competitive inhibitors?

A

they are substances that have a similar shape to the substrate and can bind and shape to the active site, blocking it and preventing it from forming ES complexes.

41
Q

what are non competitive inhibitors?

A

they are substances that can change the shape of the active site so less ES complexes can be formed

42
Q

what are 3 types of lipids?

A

triglycerides
phospholipids
cholesterol

43
Q

what are each of their roles?

A

triglycerides - they are fat for energy store and to protect the organs
phospholipids- they help with making membranes
cholesterol- for membrane stability and to make hormones.

44
Q

what is the structure of triglyceride?

A

they are made up of 1 glycerol and 3 fatty acids, and this is joined together by a condensation reaction.
there are 2 types of triglycerides, saturated fat and unsaturated.

45
Q

what is a saturated fat?

A

it has no carbon double bonds in the R group of the fatty acid

46
Q

what is an unsaturated fat?

A

it does have carbon double bonds in the R group of the fatty acid.

47
Q

what are nucleic acid?

A

polymers made from nucleotides

48
Q

what is DNA?

A

deoxyribonucleic acid, it is found in all organisms, carries your genes.

49
Q

what are genes?

A

sections of DNA that codes for a protein

50
Q

DNA structure?

A

double helix structure that joins nucleotides together by condensation and complimentary base pairs.
these produce double strands and then these coil into a double helix

51
Q

what are the properties of DNA structure?

A

double strand makes the DNA more stable, and as it coils it is more compact.
sugar phosphate backbone - protects the bases
complementary base pairing- ensures identical copies of DNA are made

52
Q

how does DNA replication occur?

A

in interphase before mitosis and meiosis, occurs by semi- conservative replication

53
Q

what is RNA?

A

RiboNucleic Acid
there are 2 types of RNA -mRNA which is messenger RNA
and tRNA- transfer RNA
they are both single stranded.

54
Q

what is ATP?

A

it is an energy carrier molecule, it delivers energy for life processes.

55
Q

what is the structure of ATP?

A

it is made from 1 adenosine and 3 phosphates, ADP + Pi + energy used = ATP

56
Q

why is ATP a good deliverer of energy?

A

it only needs to break 1 weak bond which means it is an immediate source of energy and it only releases a small amount of it which is manageable

57
Q

name some uses of ATP?

A

protein synthesis
DNA replication
Metabolic reactions
maintaining body temp

58
Q
A

human biology (6 decks)

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