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2.2-molecules Flashcards

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1
Q

What test identifies proteins ?

A

biuret test : if proteins present, colour changes from light blue to lilac.

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2
Q

What are the roles of carbohydrates?

A

1) energy store
2) energy source
3) structural unit

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3
Q

What are carbohydrates ?

A

Organic compounds only comprised of C,H, and O

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4
Q

What is the general formula of monosaccharides ?

A

CnH2n0n

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5
Q

What are isomers?

A

They have the same formula but are arranged differently in space

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6
Q

What are three examples of monosaccharides ?

A

Fructose
Glucose
Galactose

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7
Q

What bonds are formed between carbohydrates?

A

Glycosidic bonds

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8
Q

What breaks apart glycosidic bonds?

A

The addition of water and enzymes to for a hydrolysis reaction.

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9
Q

What forms sucrose ?

A

a-glucose and fructose

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10
Q

What forms lactose?

A

a-glucose and beta galactose

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11
Q

What forms maltose ?

A

2 x alpha glucose

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12
Q

What is an example of w heteropolysaccharide?

A

Hyaluronic acid

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13
Q

Why are polysaccharides good energy stores ?

A

Glycogen and starch are compact which means they don’t take up a large amount of space; they occur coiled in dense granules within the cell.
Polysaccharides hold glucose molecules in chains so they can be easily snipped off by hydrolysis.

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14
Q

Why are polysaccharides less soluble than monosaccharides ?

A

1) their size

2) regions which could hydrogen bond with water were hidden inside molecule.

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15
Q

What does amylose sometimes do to make it hydrophobic ?

A

It forms a double helix which has a hydrophobic external surface.

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16
Q

What is the structure of amylose?

A
  • long chain of a-glucose molecules
  • glycosidic bonds between carbons 1 and 4
  • spiral shape which hydrogen bonds hold in place
  • hydroxyl groups in carbon 2 are inside cell so it’s less soluble.
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17
Q

Where is glycogen stored ?

A

Dense granules in muscle and liver cells

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18
Q

Where are amylose and amylopectin stored ?

A

dense granules in starch grains in cells.

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19
Q

What is the monomer of amylose ?

A

a-glucose

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20
Q

What is the monomer of glycogen ?

A

a-glucose

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21
Q

what is the monomer of cellulose ?

A

Beta glucose

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22
Q

What is the monomer of amylopectin ?

A

a-glucose

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23
Q

Is amylose branched?

A

No

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24
Q

Is amylopectin branched ?

A

Ye

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25
Q

Is glycogen branched ?

A

Ye

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26
Q

Is cellulose branched ?

A

Nope

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27
Q

What glycosidic bonds does amylose have?

A

a1-4

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28
Q

What glycosidic bonds does amylopectin have?

A

a1-4

a1-6

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29
Q

What glycosidic bonds does glycogen have ?

A

a1-4

a1-6

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30
Q

What glycosidic bonds does cellulose have ?

A

beta 1-4

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31
Q

Is amylose spiralled?

A

Ye boi

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32
Q

Is cellulose spiralled ?

A

No

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33
Q

Is amylopectin spiralled?

A

Yeah

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34
Q

What forms a microfibril?

A

60-70 cellulose chains bound together

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35
Q

How big are microfibrils?

A

10-30nm in diameter

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36
Q

What are macrofibrils?

A

Up to 400 microfibrils

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37
Q

What are lipids ?

A

Biological molecules made of C,H, and O.

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38
Q

What are the functions of lipids?

A

1) energy source
2) energy store
3) protection
4) buoyancy
5) insulation

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39
Q

What are triglycerides made of?

A

1 glycerol

2 fatty acids

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40
Q

What are phospholipids made of ?

A

Glycerol
Phosphate
2 fatty acids

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41
Q

What does amphipathic mean?

A

A molecule that has a hydrophobic and hydrophilic side

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42
Q

What is cholesterol ?

A

A steroid alcohol

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43
Q

Where is cholesterol found in phospholipids and why?

A

It’s small and hydrophobic so found near phospholipid tails.

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44
Q

What atoms are found in proteins ?

A

N, O, C, H and sometimes suphur.

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45
Q

Why are proteins needed in organisms ?

A

Growth and repair :
Enzymes
Hormones
Structural

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46
Q

What is the secondary structure of proteins ?

A

a helix or beta pleated sheet.

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47
Q

How can the structure of amino acids be determined ?

A

1) ab initio protein modelling

2) comparative protein modelling

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48
Q

What are the bonds in proteins from strongest to weakest?

A

Ionic
Disulphide
Hydrogen

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49
Q

What is the primary structure of proteins ?

A

The sequence and order of amino acids in a polypeptide chain.

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50
Q

what are the roles of water that relate to its properties?

A

solvent
transport medium
coolant
habitat

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51
Q

what are the unusual properties of water?

A 
ice is less dense than water
high specific heat capacity 
high latent heat of vaporisation
solvent
cohesion and surface tension
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52
Q

why does ice being less dense than water help organisms?

A
  • aquatic organisms have a stable environment in which to live through winter
  • ponds and other bodies of water are insulated against extreme cold.
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53
Q

why does water being a good solvent help organisms?

A

molecules and ions can react together in water eg in cytoplasm
molecules and ions can be transported around living things while being dissolved in water.

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54
Q

why does water’s high specific heat capacity help organisms?

A
  • living things including prokaryotes and eukaryotes need a stable temperature for enzyme-controlled reactions to function.
  • aquatic organisms need a stable environment in which to live.
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55
Q

why does water being wet help organisms?

A
  • provides habitats
  • major component of tissues
  • reaction medium for chemical reactions
  • effective transport medium
56
Q

why does water’s cohesion and surface tension help organisms?

A
  • columns of water in plant vascular tissue are pulled up the xylem tissue together from the roots.
  • insects like pond skaters can skate on water.
57
Q

what is a condensation reaction?

A

when 2 molecules are joined together with the REMOVAL of water

58
Q

what is a hydrolysis reaction?

A

when 2 molecules are split apart with the ADDITION of water

59
Q

what atoms are found in carbohydrates?

A

C, H, O

60
Q

what atoms are found in lipids?

A

C, H, O

61
Q

what atoms are found in nucleic acids?

A

C, H, O,N, P

62
Q

what is the tertiary structure of proteins?

A

the overall 3D shape of the protein molecule - very precise shape held in place by bonds between amino acids.

63
Q

what is the quaternary structure of a protein?

A

protein structure which consists of more than 1 polypeptide chain

64
Q

how do h-bonds form in proteins?

A

between H atoms w/slight positive charge and other atoms with slight negative charges in hydroxyl, carboxyl, and amino groups.

65
Q

how do disulfide bonds form in proteins?

A

between sulphurs in different R groups-strong covalent bonds.

66
Q

how do ionic bonds form in proteins?

A

between carboxyl and amino groups which ionise into NH3+ and COO- groups.

67
Q

how do hydrophobic and hydrophillic interactions occur in proteins?

A

hydrophobic parts associate in centre of polypeptide to avoid water, hydrophillic parts found at edge to be clsoe to water. causes twisting of amino acid chain.

68
Q

What is an initio protein modelling?

A

Model built based on physical/ electrical properties of atoms in each amino acid in a sequence.
Can be multiple solutions to the same amino acid sequence.

69
Q

What is comparative protein modelling?

A

Scanning amino acid sequence against database of solved structures+produces set of possible models which would match that sequence.

70
Q

what bonding does cellulose have?

A

b1-4

71
Q

what happens between adjacent fibrils of cellulose in cell walls?

A

h-bonds

72
Q

why is the ability of water to act as a solvent important for the survival of organisms?

A
  • medium for metabolic reactions
  • allows ionic compounds to separate
  • can absorb/take in minerals
  • able to DILUTE toxic substances
  • transport
73
Q

what kind of bonds do triglycerides have?

A

ester bonds

74
Q

what does a balanced diet mean?

A

having all the right food groups in all the right proportions

75
Q

why does a diet high in lipids have a harmful effect on health?

A
  • obesity
  • more cholesterol–deposited in arterial walls–plaque–artery LUMEN narrows–high blood pressure, stroke, heart attack, etc
76
Q

how do you test for lipids?

A

mix thoroughly with ethanol
add cold water
if white emulsion forms, test is positive

77
Q

how is glucose well suited to its role in living organisms?

A
  • soluble so can easily be transported
  • small so can diffuse across cell membrane
  • can be quickly broken down to release energy
78
Q

how do you test for reducing sugar without a colorimeter?

A 
add benedict's + heat
forms precipitate--> blue to brick red
concentration estimate from degree of colour change/comparison with known concentration
OR centrifuge and weigh precipitate 
use standard curve
79
Q

how do you modify benedicts for non reducing sugar?

A

heat with acid, then add alkali to neutralise, then do benedicts.

80
Q

why is water having a high latent heat of evaporation good for organisms?

A

evaporation is an efficient cooling mechanism eg sweating

81
Q

why does water being transparent help organisms?

A

allows underwater photosynthesis

82
Q

why does water’s high density help organisms?

A

allows flotation

83
Q

What does calcium do?

A
  • involved in transmitting nerve impulses
  • important in blood clotting and muscle contraction
  • increases rigidity of bones, teeth, and cartilage
84
Q

What does sodium do?

A
  • involved in regulation of osmotic pressure, control of water levels in body fluid and maintenance of pH.
  • important for generating nerve impulses
  • contributes to muscle contraction.
85
Q

What does potassium do?

A
  • involved in control of water levels in body fluid+ maintenance of pH.
  • assists active transport of materials across cell memebrane
  • important for generating nerve impulses and muscle contraction
  • generates healthy flowers+leaves in flowering plants
86
Q

What does H+ do?

A
  • Involved in photosynthesis and respiration
  • involved in transport of O2 and CO2 in blood
  • involved in regulation of blood pH.
87
Q

What does ammonium do?

A
  • component of amino acids, proteins, vitamins, and chlorophyll
  • component of nitrogen cycle
  • maintaining blood pH in human body
88
Q

What does nitrate do?

A
  • component of nitrogen cycle

- component of amino acids, proteins, vitamins, and chlorophyll

89
Q

What does HCO3- do?

A
  • regulation of blood pH

- transport of CO2 into+ out of blood

90
Q

What does chloride do?

A
  • regulates blood pH (chloride shift)
  • helps in production of urine from kidney+maintenance of blood pH.
  • uses to produce HCl in stomach.
91
Q

What does phosphate do?

A
  • component of nucleic acids, ATP, phospholipids, and some enzymes
  • increases rigidity of bone, teeth+cartilage (calcium phosphate)
  • helps root growth in plants
92
Q

What does OH- do?

A

Regulates blood pH.

93
Q

What is the phosphate ion?

A

PO4 3-

94
Q

state 5 roles of cholesterol in living organisms

A

1) maintaining fluidity of cell membranes
2) making vitamin D
3) making bile
4) converted to steroid hormones
5) waterproofing skin

95
Q

why is glycogen a good storage molecule?

A

compact-lots of energy per volume-energy dense
lots of branches for enzymes to attach
insoluble-doesn’t affect water potential of cell
easily hydrolysed

96
Q

what bonding does glycogen have?

A

a1-4 and a1-6

97
Q

what are the axissessesse (?) of a calibration curve?

A

percent transmittance/absorbance and concentration

98
Q

what’s the link between chlorine and amylase?

A

chloride ion is a COFACTOR of amylase

99
Q

what are the positions of hydrophobic and hydrophillic groups in haemoglobin?

A

hydrophillic on outside

hydrophobic r groups on inside

100
Q

what is the haem group in haemoglobin acting as?

A

PROSTHETIC GROUP

101
Q

what kind of bond forms between glycerol and fatty acid?

A

ester bond

102
Q

how does heat affect the tertiary structure of a protein?

A 
cause molecules to have more kinetic energy
vibrate more
namedbondsbreak
change in 3D shape of protein
protein denatures
103
Q

what are 4 properties of collagen that make it good for ligaments between muscles and bones?

A

strong
flexible
insoluble
not elastic

104
Q

what are 5 properties of cellulose that make it suitable for a plant cell wall?

A 
insoluble
high tensile strength-never say strong all alone!!
unreactive/inert
flexible
can form h-bonds w neighbouring chains
105
Q

what forms cellubiose?

A

b glucose +b glucose

106
Q

what are bacteria cell walls made of?

A

peptodoglycan-long polysaccharide chains crosslinked by short peptide chains

107
Q

what are exoskeletons made of?

A

chitin

108
Q

what are examples of lipids?

A

triglycerides
phospholipids
glycolipids
cholesterol

109
Q

what is a monounsaturated fatty acid?

A

one that has only 1 double CC bond

110
Q

what is a polyunsaturated fatty acid?

A

one that has more than 1 double CC bond

111
Q

where is cholesterol made in animals?

A

mainly the liver

112
Q

what are examples of steroid hormones made from cholesterol?

A

testosterone
oestrogen
vitamin D

113
Q

what is the secondary structure of proteins?

A

the coiling or folding of an amino acid chain, which arises often as a result of h bond formation between diff parts of the chain-mian forms = a helix and b pleated sheet.

114
Q

what bonds form within proteins?

A

h bonds
ionic
disulfide
hydriphobic/hydrophillic interactions

115
Q

what are the properties of fibrous proteins?

A

regular repetitive AA sequences
insoluble
form fibres

116
Q

what are the properties of globular proteins?

A

spherical
soluble-hydrophobic on inside
specific shapes eg enzymes

117
Q

what is the function of collagen?

A

to provide mechanical strength

118
Q

what are examples of places collagen is found?

A

artery walls
tendons
bones
cartilage/connective tissue

119
Q

why is keratin strong?

A

rich in cysteine: lots of disulfide bridges.

120
Q

where is keratin found?

A

fingernails, hair, hoofs, horns, scales, fur, feathers.

121
Q

what is the purpose of keratin?

A

mechanical protection
impermeable barrier to infection
waterproof

122
Q

what makes elastin strong and extensible?

A

cross linking and coiling

123
Q

where is elastin found?

A

skin
lungs
bladder
blood vessel walls

124
Q

what is the quaternary structure of haemoglobin?

A

4 polypeptides: 2a, 2b. on each chain there’s a haem group.

125
Q

what is a protein with an ion prosthetic group called?

A

conjugated protein

126
Q

how many polypeptide chains is insulin made of?

A

2

127
Q

is insulin soluble?

A

yeah

128
Q

what is the structure of pepsin?

A

1 polypeptide chain, symmetrical tertiary structure

129
Q

how do you test for starch?

A

add iodide solution-yellow brown to blue black.

130
Q

WHAT DOES REPEATING EXPERIMENTS DO

A

ALLOWS YOU TO IDENTIFY OUTLIERS, IMPROVING RELIABILITY, LETTING YOU CALCULATE SPREAD OF RESULTS, AND ALLOWING CALCULATION OF THE MEAN.

131
Q

DO PHOSPHOLIPIDS CONTAIN GLYCEROL

A

NO

132
Q

DOES CHOLESTEROL CONTAIN ESTER BONDS

A

NO

133
Q

WHAT MIGHT BE DIFFERENT ABOUT THE FAKE MEAT PRODUCED BY MICROORGANISMS COMPARED TO NORMAL MEAT ?

A

THE FAKE ONE WOULD HAVE LESS SATURATED FAT AND MORE UNSATURATED FAT.

134
Q

WHAT DO ALPHA AND BETA SUBUNITS CONNOTE

A

THE QUATERNARY STRUCTURE!! THE DIFFERENT CHAINS.

135
Q

WHAT DOES OVERALL 3D SHAPE CONNOTE

A

TERTIARY STRUCTURE

136
Q

WHERE ARE HAEMOGLOBIN’S HYDROPHILLIC GROUPS?

A

ON THE OUTSIDE.

Biology (25 decks)

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