Module 2.2 Flashcards

Biological molecules

1
Q

Why can water hydrogen bond

A

Oxygen has more protons in its nucleus than hydrogen (more electronegative)
The shared electrons are attracted slightly towards the oxygen nucleus
The oxygen becomes delta negative
Hydrogen becomes delta positive
H bonds between hydrogen and oxygen of separate molecules

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2
Q

Properties of water from H bonds

A

High SHC
Density
High latent heat of vaporisation
Adhesion and cohesion
Solvent
Liquid

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3
Q

Why is high SHC good

A

It is difficult to heat water up
provides stable habitat
Stable temperature for enzymes

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4
Q

Why is high latent heat of vaporisation good

A

Helps with cooling from sweat/panting

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5
Q

Why is density good

A

Ice is less dense than water
Difficult for whole bodies of water to freeze (animals can live under the ice)
Ice acts as an insulating layer (stable environment underneath)
Floating ice is habitat for other animals

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6
Q

Why is a solvent good

A

Transport medium
Substances dissolved in it can react (cytoplasm)

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7
Q

Why is adhesion and cohesion good

A

In the xylem
surface tension provides habitats for insects (pond skaters)

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8
Q

Why is liquid good

A

Transport medium
dissolved substances can move around

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9
Q

What is a monomer

A

the subunit(s) used to form a polymer when more than one is joined together

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10
Q

What is a polymer

A

A molecule consisting of more than one molecule joined together

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11
Q

What is a condensation reaction

A

The joining of two molecules
Water is removed

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12
Q

What is a hydrolysis reaction

A

The breaking apart of molecules
Uses up water

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13
Q

Element in carbohydrates

A

C,H,O

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14
Q

Elements in proteins

A

C,H,O,N,S

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15
Q

Elements in lipids

A

C,H,O

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16
Q

Elements in nucleic acids

A

C,H,O,N,P

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17
Q

Structure of amylopectin

A

Formed of a-glucose monomers
Branched 1-4 and 1-6 bonds
in a spiral shape
insoluble

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18
Q

Amylose structure

A

Formed of a-glucose monomers
Not branched 1-4 bonds only
Coiled
insoluble

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19
Q

Glycogen structure

A

Formed of a-glucose monomers
Highly branched 1-4 and 1-6 bonds
Less coiled
Insoluble

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20
Q

Cellulose structure

A

Formed of b-glucose monomers
straight chains because of OH on top in b-glucose
Alternating monomer are rotated 180
Can H-bond between chains
Insoluble

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21
Q

Function of glycogen, amylose and amylopectin

A

Energy storage glycogen=animals starch (amylose and amylopectin) = plants
Insoluble as OH group on inside of coil so don’t affect the water potential of the cells
Amylopectin and glycogen are branched to provide more hydrolysis points to remove glucose from the molecule (more energy per unit time)
Glycogen in most branched as it is in animals which are more metabolically active
Compact so don’t take up space
Glucose easily snipped off

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22
Q

Monomers of sucrose

A

Fructose and glucose

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23
Q

Monomers of maltose

A

2 glucose molecules

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24
Q

Monomers of lactose

A

galactose and glucose

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25
Q

Triglyceride monomers

A

Glycerol, 3 fatty acids

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26
Q

Phospholipid monomers

A

Glycerol, phosphate, 2 fatty acids

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27
Q

difference between saturated and unsaturated fatty acids

A

Saturated have the maximum C-H bonds
Unsaturated have one or more double C bonds so have a kink
Kink means unsaturated are more liquid as tails means it is harder to compress into a liquid

28
Q

Bond name between 2 or more monosaccharides

A

Glycosidic bond

29
Q

Bond name between glycerol and fatty acids

A

Ester bond

30
Q

Triglyceride function

A

Buoyancy
Protection of organs
Insulation (heat and electrical)
Energy storage (insoluble)
Energy source (can produce 2x as much energy as glucose)

31
Q

Phospholipid function

A

Phosphate head is hydrophilic
Fatty acid tails are hydrophobic
Make up the plasma membrane (partially permeable as only small non-polar molecules can pass through tails)

32
Q

Cholesterol structure

A

4 carbon based rings

33
Q

Cholesterol function

A

Regulates fluidity of the plasma membrane
Makes up steroid hormones
Is hydrophobic

34
Q

Bond name between amino acids

A

Peptide bonds

35
Q

Primary protein structure

A

The sequence of amino acids
Peptide bonds

36
Q

Secondary protein structure

A

Initial folding
Alpha-helix (mainly globular)
Beta-pleated sheet (Mainly fibrous)
Hydrogen bonds

37
Q

Tertiary protein structure

A

Folding into 3D shape
Hydrophobic/philic interactions (group together, phobic go inside philic go outside of molecule)
Disulphide bridges (only between cysteine)
Ionic bonds
H bonds

38
Q

Quaternary protein structure

A

Only in some proteins
Joining of more than one polypeptide molecules

39
Q

Structure of haemoglobin

A

2 globin chains
2 globin chains
4 haem groups (contains Fe+ ion) (prosthetic group)

40
Q

Function of haemoglobin

A

Haem group bonds with oxygen to transport it in the blood to respiring tissues

41
Q

Structure of insulin

A

2 polypeptide chains
alpha chain starts with a-helix
Beta chain ends with b-pleated sheet

42
Q

Insulin function

A

Controls blood sugar by binding to glycoprotein receptors on cells to increase their uptake of glucose from the blood
Soluble so can travel in the blood

43
Q

What is a conjugated protein

A

Globular protein with a prosthetic group e.g. haemoglobin

44
Q

Collagen properties

A

Mechanical strength

45
Q

Collagen function

A

Around artery walls to prevent bursting
Tendons
Bonds
Cartilage and connective tissues

46
Q

Keratin properties

A

Insoluble and impermeable
very strong

47
Q

Keratin function

A

Impermeable barrier to infection
Prevents entry of water-borne pollutants
Mechanical protection

48
Q

Elastin properties

A

Strong
Extensible

49
Q

Elastin function

A

Stretch and recoil of skin, bladder and alveoli
Helps blood vessels stretch and recoil maintaining blood pressure

50
Q

What does biuret test for

51
Q

Biuret positive result

A

Blue to lilac

52
Q

How to carry out biuret test

A

Add sample to a spotting tile
Add biuret

53
Q

What does benedict’s solution test for

A

Reducing sugars

54
Q

Benedict’s positive result

A

Blue to green/yellow/orange/brick red depending on concentration of reducing sugar

55
Q

How to carry out benedict’s test

A

Add sample to a test tube
Add benedict’s solution
Heat in a water bath to at least 80 degrees for 3 mins

56
Q

How to test for non-reducing sugars

A

Do normal benedict’s test first
Add sample to test tube
Add hydrochloric acid to sample
Heat in a water bath to a boil
Neutralise with sodium hydrogen carbonate until fizzing stops
Add benedict’s solution
Heat to at least 80 degrees

57
Q

What does iodine test for

58
Q

Iodine positive result

A

Yellow to blue/black

59
Q

How to carry out starch test

A

Add sample to spotting tile
Add iodine

60
Q

What does emulsion test for

61
Q

Emulsion test positive result

A

White cloudy layer on top of solution

62
Q

How to carry out emulsion test

A

Add sample to test tube
mix sample with ethanol
filter
Pour solution into water
leave to settle

63
Q

How to determine concentration of substance - colorimetry

A

serial dilution of known concentration
Set colorimeter to red
Calibrate with distilled water
Test absorption for known concentrations
Plot calibration curve
Test absorption for unknown
Find absorption for unknown on calibration curve then down to concentration

64
Q

R value calculation

A

Distance moved by the solute / distance moved by the solvent

65
Q

Cellulose cell wall function

A

Plant cell walls
High tensile strength prevents cells from bursting when turgid
Criss cross wall for extra strength
Space between microfibrils making it fully permeable for water and mineral ions to pass through
Cellulose embedded in pectin
Can be reinforced with waxes (suberin, cutin) for waterproofing

66
Q

Pepsin structure

A

Single polypeptide chain
Has very few basic R-groups
Mainly acidic R-groups so is stable in the stomach as acidic R-groups cannot accept H+ ions

67
Q

Pepsin function

A

Digests protein
In the stomach