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AS biology > 2.2.6-14 biomols - lipids, proteins, inorganic ions > Flashcards

2.2.6-14 biomols - lipids, proteins, inorganic ions Flashcards

1
Q

lipids are only soluble in …

A

ORGANIC solvents

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2
Q

saturated lipids

A
  • eg animal fats (solid)
  • only c-c single bonds
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3
Q

unsaturated lipids

A
  • eg plant oils (FOREXAMPLE SAY VEGETABLE OIL ) (liquid)
  • c=c double bonds
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4
Q

unsaturated lipid melting point

A

LOWER
- double bond causes a kink in the chain
- molecules cant pack as closely together
- weaker imfs so lower mp

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5
Q

unsaturated lipid state (room temp)

A

liquid

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6
Q

saturated lipid state (room temp)

A

solid

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7
Q

triglycerides

A

lipids made of one glycerol headand 3 fatty acid tails

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8
Q

bond joining glycerol and fatty acids

A

ester bond

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9
Q

reaction where triglycerides are made

A

condensation

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10
Q

use of triglycerides

A

ENERGY STORAGE (plant + animals)

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11
Q

phospholipids

A
  • one fatty acid of a triglyceride is replaced by a phosphate containing group
  • glycerolhead, 2 fatty acid chains, 1 phosphate
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12
Q

phosphate head property…

A

HYDORPHILIC (as it is charged)

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13
Q

tail of phospholipid property

A

HYDROPHOBIC

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14
Q

hydrogen ion formula

A

H+

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15
Q

amino group

A

NH2

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16
Q

how many diff amino acids

A

20
- differ by their ‘R’ group

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17
Q

bond joining amino acids

A

PEPTIDE bond

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18
Q

reaction joining amino acids

A

condensation

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19
Q

primary structure (2)

A

-order and number of amino acids in a protein
- held together by PEPTIDE bonds

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20
Q

secondary structure

A

-REGULAR FOLDING of amino acid chain into repeating patterns
- either alpha helix or beta pleated

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21
Q

what bond holds together secondary structure

A

hydrogen bonding

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22
Q

tertiary structure of proteins

A
  • SECONDARY IS COILED AND FOLDED FURTHER
    -disulfide bridge, ionic, hydrogen bonds between R GROUPS !!!!!!!!!
  • FINAL 3D STRUCTURE OF AMINO ACIDS FROM 1 PPC
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23
Q

globular protein shape

A

highly folded - spherical

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24
Q

examples of fibrous (2)

A
  • keratin
  • collagen
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25
Q

example of globular (3)

A
  • haemoglobin
  • insulin
  • enzymes
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26
Q

biuret test

A
  • add BIURET
    OR
  • sample + equal amount of NaOH
  • add copper (II) sulphate solution and mix
  • if positive, blue -> lilac
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27
Q

lipids test

A
  • add ethanol and thoroughly shake
  • add water
  • if positive, colourless -> milky white
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28
Q

macromolecules

A

complex molecules with a high mr

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29
Q

lipids elements

A

carbon, hydrogen, oxygen

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30
Q

why are lipids insoluble in water

A

hydrophobic tail

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31
Q

break down of triglycerides reaction

A

hydrolysis

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32
Q

why are triglycerides good for storage (2)

A
  • long HC tails of fatty acids contain lots of chemical energy. lipids contain 2x as much energy per gram as carbohydrates
  • insoluble, dont change osmotic conditions.
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33
Q

where are phospholipids found

A

cell membranes of all eukaryotes and prokaryotes (phospholipid bilayer)

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34
Q

phospholipid bilayer

A
  • phospholipid heads are hydrophilic, and tails hydrophobic, so they form a double layer with their heads facing out towards the water on either side
  • centre of the layer is hydrophobic, so membrane is a barrier
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35
Q

cholesterol

A

4 ring structure

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36
Q

cholesterol size + shape

A

small size + flattened shape, so cholesterol can fit in-between phospholipid molecules of membrane

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37
Q

dipeptide

A

2 amino acids join together

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38
Q

amino acid elements

A

CHON(S)

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39
Q

Quaternary structure

A
  • diff PPC held together by bonds
  • the way the chains are assembled together
  • eg haemoglobin from 4 PPCS
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40
Q

globular solubility and why

A

SOLUBLE (so easily transported)
- hydrophilic R groups pushed to the outside, hydrophobic on inside
- forms HB with water

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41
Q

haemoglobin

A
  • globular
  • carries oxygen around the body in RBCs
  • 2 alpha 2 beta
  • conjugated protein; EACH PPC SUBUNIT has a non protein (prosthetic) group attached - 4 prosthetics
  • called, haem, which contains the single Fe2+ ion that oxygen binds to
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42
Q

are lipids polymers

A

NO

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43
Q

are lipids soluble

A

NO
- dont affect cell water potential , or osmosis

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44
Q

Lipid purposes (7)

A
  • thermal insulation (blubber)
  • electrical insulation (myelin sheath)
  • energy store
  • protection of organs (waxy cuticle, fat)
  • cell membranes (phospholipid bilayer)
  • steroid hormones (eg testosterone)
  • source of water (respiration)
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45
Q

why do camels store fat in their humps

A
  • lipids can be broken down in aerobic respiration to release energy
  • creating water
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46
Q

blubber provides (2)

A
  • warmth
  • buoyancy
47
Q

bonds holding together amino acids in primary structure

A

peptide bonds

48
Q

what bonds hold secondary structures together

A

Hydrogen bonds

49
Q

bonds holding tertiary structures together

A
  • HBs between polar R groups
  • ionic bonds between R groups
  • covalent disulphide bonds between two R groups with sulfur
50
Q

fibrous solubility

A

insoluble
few hydrophilic groups

51
Q

fibrous level of structure

A

quaternary

52
Q

why are fibrous strong

A

bonding between polypeptide chains

53
Q

collagen structure (6)

A

CHON
- peptide bonds between amino acids
- every 3rd amino acid is glycine
- 3 PPCS
- h bonds between chains
- adjacent chains form covalent bonds (crosslinks) which are staggered to avoid weak points
- insoluble, as few hpi groups on outside

54
Q

collagen uses (4)

A
  • artery walls to withstand high BP
  • tendons
  • bones
    -cartilage
55
Q

keratin structure

A

2 PPCS

56
Q

NH4+ (2)

A
  • nitrogen cycle
  • maintains pH
57
Q

Ca2+ (3)

A
  • blood clotting
  • activates enzymes
  • stimulates muscle contraction
58
Q

why not do emulsion test on something cloudy

A

cant see If result is positive or not

59
Q

why do lipids release lots of energy

A

high energy: mass ratio , so high calorific value from oxidation

60
Q

lipids insolubility advatanges (2)

A
  • waterproofing
  • no effect on WP of cells
61
Q

lipids conduction of heat

A

slow
thermal insulation

62
Q

lipids buoyancy of animals

A

less dense than water

63
Q

elastin uses

A
  • elasticity to connective tissue
  • arteries, skin, lungs etc
64
Q

what is buret made of

A

sodium hydroxide + copper sulfate

64
Q

NO3-

A
  • DNA + amino acids
65
Q

OH-

A
  • maintain pH
  • cause denaturation
66
Q

PO43-

A
  • DNA
67
Q

hydrocarbon tail solubility

A

INSOLUBLE
Hydrophobic

68
Q

number of waters formed for each triglyceride

A

3

69
Q

how to triglycerides clump together

A

in DROPLETS
Hydrophobic carbon tails face out

70
Q

cholesterol role

A
  • reduces fluidity of **eukaryotic **cell membranes
  • phospholipids more tightly packed so membrane is more rigid
71
Q

all steroid hormones are derived from

A

cholesterol

72
Q

how does a phospholipid differ to triglyceride

A

one of the 3 fatty acid chains is replaced by a phosphate molecule

73
Q

‘R’ group significance

A
  • variable group
  • gives amino acid its specific characteristics
74
Q

are enzymes globular or fibrous

A

globular

75
Q

sulfer atoms needed for …

A

proteins

76
Q

Conjugated protein defintion

A
  • has a non protein
  • prosthetic group
    -attached by covalent bonds
  • specify what it is (eg fe2+)
77
Q

how many prosthetic groups in haemoglobin

A

4

78
Q

properties of fibrous (4)

A
  • little tertiary structure - ELONGATED
  • insoluble
  • small range of amino acids
  • STRONG
  • flexible
  • structural (collagen)+protective (keratin) functions
79
Q

WHY is collagen so strong

A
  • hydrogen bonds
  • cross links [covalent bonds]
80
Q

cytseine special feature

A

SULFUR - disulfide bridge

81
Q

chromatography comparison (4)

A
  • blots of the 2 samples
  • separate with a solvent
  • NINHYDRIN stain to see spots
  • compare patterns
82
Q

describe peptide bond

A

between AMINE group and CARBOXYL group of adjacent amino acid

83
Q

4 key features of collagen

A
  • high tensile strength
  • inelastic
  • insoluble
    -flexible
84
Q

suggest how plasmodium releases amino acids from haemoglobin

A
  • hydrolysis
  • by enzymes (proteases)
  • peptide bonds broken
85
Q

explain how the structure of phospholipids allows them to form the bilayer of a plasma membrane? (5)

A
  • hydrophilic phosphate head and hydrophobic fatty acid tails
    -hydrophobic tails are repelled by water
  • hydrophilic head forms H bonds with water
  • MEDIUM OUTSIDE MEMBRANE IS AQUEOUS
    -hydrophobic tails mean they face towards each other
86
Q

circle ester bond

A

both O atoms and the C between them

87
Q

density of lipids v proteins

A

lipids are less dense than proteins

88
Q

bile is made of

A

cholesterol

89
Q

hydrolysis of triglycerides

A
  • use of water
  • to break 3 ester bonds
  • forming glycerol + 3 fatty acids
90
Q

enzyme’s biuret

A
  • positive
  • is possible because enzymes are globular so soluble
91
Q

similarities in phospholipids and triglycerides?

A
  • contain glycerol
  • fatty acids
  • ester bonds
  • C,H,O
92
Q

PEPTIDE BOND ATOM FORMATION

A

H from amine with OH from carboxyl

93
Q

test solid for proteins

A
  • crush a small amount
  • add biurets
  • blue to lilac
94
Q

collagen atoms

A

C,H,O,N

95
Q

crosslinks in collagen

A
  • covalent bonds between the 3 adjacent molecules
  • staggered at the end of molecules to avoid weak points
96
Q

how to know if its unsaturated with just molecular formula

A

LOWER RATIO of hydrogens to oxygens

97
Q

what type of bond is a peptide bond

A

COVALENT

98
Q

globular proteins temperature

A

very sensitive
shape easily distorted

99
Q

amylase ion

A

calcium ion

100
Q

insulin

A
  • fixed specific shape
  • 2 PPCs with disulphide bridges
  • soluble
101
Q

ammonium (3)

A
  • amino acids
  • nitrogen cycle
    -pH
102
Q

ca 2+ (2)

A
  • blood clotting
  • activates enzymes
103
Q

h+

A
  • regulation of blood pH
  • transport of CO2 in blood
104
Q

fe2+

A

increases affinity of haemoglobin for oxygen

105
Q

na+

A
  • regulation of water potential in cells and bodily fluids
  • reabsorption of water in kidney
106
Q

mg2+

A

chlorophyll

107
Q

k+

A
  • growth of leaves and flowers
  • regulation of water p in cells and bodily fluids
108
Q

cl-

A
  • reabsorption of water in kidney
  • production of HCl in stomach
109
Q

HCO3-

A
  • regulation of blood pH
  • transport of co2 in blood
110
Q

OH-

A

regulation of blood pH

111
Q

no3=

A
  • nitrogen cycle
  • amino acids, proteins, nucleic acids
112
Q

po43-

A
  • component of phospholipids and atp
113
Q

globular properties

A
  • soluble
  • spherical
  • HAVE 3D TERTIARY STRUCTURE
  • temperature+pH sensitive
  • metabolic role (enzymes), transporting substances (haemoglobin)

AS biology (14 decks)

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