Biological Molecules Flashcards

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1
Q

Momomer of carbohydrates

A

Monosaccharides

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2
Q

2 polysaccharides in starch

A

Amylose and amylopectin

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3
Q

Describe structure of amylose

A

Unbranched
Alpha glucose
Coiled = angles of glycosidic bonds (1,4)

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4
Q

Describe structure of amylopectin

A

Branched

Alpha glucose

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5
Q

Why is starch going for plant storage

A
Amylose = coiled = compact 
Amylopectin = highly branched = enzymes break glycosidic bonds quickly
Insoluble = doesn’t affect water potential
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6
Q

What is the test fir starch

A

Iodine dissolved in potassium idiode

Orange -> blue/black

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7
Q

Describe structure of glycogen

A

Alpha glucose

Highly branched

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8
Q

How is glycogen adapted for its function

A

Highly branched = enzymes can break glycosidic bonds quickly and release e
Compact

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9
Q

Describe the structure if cellulose

A

Unbranched
B glucose
Straight chains linked my H bonds
Every other glucose flips

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10
Q

How does cellulose provide structure and support

A

H bonds link chains

Form microfibrils

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11
Q

What is the structure of triglycerides

A

Glycerol + 3 fatty acids

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12
Q

What is a fatty acid

A

Hydrophobic hydrocarbon chain

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13
Q

How does a triglyceride form

A

Condensation reaction

Forms ester bond with glycerol and fatty acid

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14
Q

What are saturated fatty acids

A

No double bonds

Max no of H

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15
Q

Why do unsaturated fatty acids kink

A

Double bond

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16
Q

What is the structure of a phospholipid

A

1 glycerol + 1 phosphate group + 2 fatty acids

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17
Q

Is the phosphate group hydrophobic

A

No - it’s hydrophilic

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18
Q

What is the function of triglycerides

A

Energy storage

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19
Q

Why are triglycerides good for their function

A

Long hydrocarbon tails release lots of energy when broken down = 2x amount In same mass of carbs

Insoluble = dont affect water potential

               =  clump together in insoluble droplets because fatty acids are hydrophobic
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20
Q

What is the function of phospholipids

A

Bilayer of plasma membrane

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21
Q

Describe the emulsion test fir lipids

A

Add ethanol
Shake for 1 min
Pour into water
Lipid = milky

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22
Q

How to know if there’s more lipid in a food

A

More milky emulsion

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23
Q

What is the monomer of proteins

A

Amino acids

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24
Q

What is the structure of amino acids

A

Amine group
Carboxyl group
Variable group

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25
Q

What is the bond that joins amino acids

A

Peptide bonds

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26
Q

What type of reaction is the formation of polypeptides

A

Condensation

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27
Q

Describe the primary structure of a protein

A

Séquence of amino acids

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28
Q

Describe the secondary structure of a protein

A

H bonds form between amino acids
Coil = a helix
Fold = b pleated sheets

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29
Q

Describe the tertiary structure of a protein

A

More bonds forms between amino acids
H bonds
Ionic bonds
Disulfide bridges

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30
Q

Describe the quarternary structure of a protein

A

Multiple polypeptide chains bonded together

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31
Q

What amino acids form disulphide bridges

A

Cysteine

32
Q

Why are keratin and collagen structural proteins

A

Polypeptide chains are parallel to each other

Form cross links

33
Q

Give 4 uses of proteins

A

Enzymes
Structural proteins
Antibodies
Transport proteins

34
Q

Describe the buiret test

A
Add NaOH
Add Cu(II)SO4
\+ve = purple 
-ve = blue
35
Q

What is the Biuret test for

A

Proteins

36
Q

Where is enzyme action

A

Intracellular (inside cell) and extra cellular (outside cell)

37
Q

Why are enzymes highly specific

A

Tertiary structure

38
Q

What forms when a substrate and enzyme bind

A

Enzyme-substrate complex

39
Q

What do enzymes do when 2 molecules need to be joined

A

Both attached to the same enzyme
Held close together
Reducing repulsion
Bond more easy

40
Q

What does the enzyme do when 2 molecules need to break up

A

Fitting into the AS causes stress on bonds in the substrate

Breaks more easily

41
Q

What is the lock and key model

A

Specific Substrate fits into the specific AS

42
Q

What is the induced fit model

A

Enzyme binds to substrate
Enzyme-substrate complex changes shape slightly to complete fit
Locks substrate more tightly

43
Q

Why does the tertiary structure affect the AS

A

Tertiary structure determine AS

every enzyme has different tertiary structure = different AS

44
Q

What happens if the tertiary structure of the enzyme changes

A

AS changes shape
Substrate won’t fit
Can’t form enzyme-substrate complex

45
Q

How can a gene mutation affect enzyme function

A

Change amino acid gene codes for
Different primary structure
Different tertiary structure

46
Q

What is a competitive inhibitor

A

Similar shape to substrate
Compete to bind to AS
blocks substrate from binding
Slows rate of reaction

47
Q

Does increasing conc of sub affect the rate of reaction with a competent be inhibitor

A

Yes

The substrate has more chance of binding to the AS

48
Q

What is a non competitive inhibitor

A

Bind away from AS
AS changes chape
Substrate can’t bind = AS no Longer complimentary

49
Q

Will increasing conc of sub affect rate of reaction with a non comp inhibitor

A

No

Once the enzyme has been denatured it can’t bind to the sub

50
Q

What is the monomor of dna

A

Nucleotides

51
Q

What is in a DNA nucleotide

A

Pentose sugar (deoxyribose)
Base containing N
Phosphate group

52
Q

Give 2 difference between rna and dna nucleotides

A

Oxyribose not deoxyribose

Uracil not tymine

53
Q

What bond forms between nucleotides

A

Phosphodiester bonds

54
Q

What is the chain of sugars and phosphate in dna

A

Sugar phosphate backbone

55
Q

How many H bonds between c and g

A

3

56
Q

How many H bonds between T and A

A

2

57
Q

Why does dna form a double helix

A

H bonds between complementary base pairs

On strands going antiparallel

58
Q

Describe dna semi conservative replication

A
  1. Dna helicase break h bonds between complementary base pairs
  2. Helix unwinds
  3. Each original strand is a template for a new
  4. Free floating nucleotides join to complementary base pairs attracted to Éxposed bases
  5. DNA polymerase catalysés condensation reaction to form H bonds between bases
59
Q

What is semi conservative replication

A

Each new dna molecule contains 1 strand from original and 1 new

60
Q

Why is replication semi conservative

A

Maintain Genetic continuity

61
Q

Why does anti parallel strands affect DNA polymerase

A

DNA polymerase can only complementary to 3’
Nucleotides only added to 3’ end
So it binds to the original strands 3’ end
New = works from 5’ to 3’

So the DNA polymerase works in opposite directions

62
Q

Describe the experiment that proved semi conservative replication

A
  1. 2 samples of bacteria grown
  2. 1 grown in N14 and 1 in N15
  3. Bacteria reproduced taking up the N in dna
  4. Sample of dna taken and spun in centrifuge
  5. N15 settled lower
  6. Bacteria grown in N15 put into N14
  7. Allowed 1 round of replication
  8. Dna taken and spun in centrifuge
  9. DNA settled inbetween N15 and N14 because it had 1 strand of each
63
Q

Why is water a good metabolite

A

Used in condensation and hydrolysis reactions

64
Q

Why is water a good at temp control

A

High latent heat of vaporisation = takes lots of energy to break h bonds between water molecules = lots of energy used when it evaporates
Eg. Sweat

65
Q

Why can water buffer temp changes

A

High specific heat capacity = H bonds between molecules can absorb lots of energy
No rapid temp changes
Good habitat for marine life
Good inside body = maintain constant body temp

66
Q

Why is water a good solvent

A

It’s polar

So surrounds ions

67
Q

Why is water good at moving up a plant

A

It’s cohesive because they’re polar
Strong attraction between molecules
Helps pull whole water column in xylem

68
Q

Why does sweat form droplets

A

Strong cohesion = string surface tension when water is in contact with air
Droplets can evaporate to cool skin

69
Q

What is the structure of ATP

A

Adenine
Ribose
3 phosphate groups

70
Q

Why is atp a nucleotide derivitive

A

Modified nucleotide

71
Q

Why is glucose turned into atp

A

Cells can’t get energy directly from glucose

72
Q

What is the reaction for energy release from atp

A

Atp → adp + pi

Hydrolysis

73
Q

Where is energy released from atp

A

The bond breaking between 2 phosphate groups

74
Q

What is the break down of atp catalysed by

A

Atp hydrolase

75
Q

What is the formation of atp catalysed by

A

Atp synthase

76
Q

What does it mean by atp hydrolysis can be “coupled”

A

Energy released from atp can be directly used to an energy needed reaction so it’s not lost by heat

77
Q

What can the Pi be used as

A

Can be added to other compounds (phosphorylation)

Make them more reactive