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Biology > Biological Molecules > Flashcards

Biological Molecules Flashcards

1
Q

What is a monomer

A

The smaller units from which larger molecules are made

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2
Q

What are polymers

A

A chain of lots of monomers joined together

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3
Q

What is a condensation reaction

A

A reaction which joins two molecules together, which forms a chemical bond and involves the elimination of a water molecule

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4
Q

What is a hydrolysis reaction

A

A reaction which breaks a chemical bond between two molecules and seperates them, this involves the use of a water molecule

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5
Q

Are linear or ring monosaccharides more common?

A

Ring

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6
Q

What are the 3 classes of carbohydrates and how many sugar units do they contain?

A

Monosaccharide - 1
Disaccharide - 2
Polysaccharide - Many

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7
Q

What is the name of a monosaccharide with 3, 5 and 6 carbon atoms

A

3 - Triose
5 - Pentose
6 - Hexose

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8
Q

What are the two functional groups found in monosaccharides

A

Ketone group (ketose sugar)
Aldehyde group (aldose sugar)

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9
Q

what does the ketone group look like

A

Ketone has a carbonyl group
O
||
C - C - C

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10
Q

What does the Aldehyde functional group look like

A

Aldehyde has a carbonyl group
O
||
C - H

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11
Q

What does the carbonyl functional group look like?

A

O
||
C

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12
Q

what does the hydroxyl group look like

A

O - H

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13
Q

What does R represent in displayed formulas

A

Hydrocarbon chain

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14
Q

What are monosaccharides

A

The monomers from which larger carbohydrates are made

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15
Q

Why can’t monosaccharides be hydrolised?

A

They are already the most basic sugar unit

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16
Q

What are 4 characteristics of monosaccharides

A

Colourless
Water soluble
Crystalline solids
Sweet taste

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17
Q

What are the 3 monosaccharides

A

glucose
galactose
fructose

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18
Q

what is the difference between fructose and glucose/galactose

A

fructose is a 5 membered ring, the other 2 are 6 membered rings

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19
Q

What is the structure of galactose

A

C4 has OH on top and H below

https://www.google.com/search?q=GALACTOSE+IMAGE&client=firefox-b-d&sca_esv=9029f727d4831701&biw=766&bih=776&sxsrf=ADLYWIKvjCeGLDUwNbeiZAhyN4XCNKsBuA%3A1735031735770&ei=t3tqZ8LdLrC_hbIP-q7gMA&ved=0ahUKEwiClaPyiMCKAxWwX0EAHXoXGAYQ4dUDCBA&uact=5&oq=GALACTOSE+IMAGE&gs_lp=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&sclient=gws-wiz-serp

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20
Q

Why are monosaccharides important (3)

A
  • They are the major nutrients of cells which provide energy for cellular respiration
  • They are the monomers for the synthesis of disaccharides and polysaccharides
  • They are the raw material for the synthesis of other monomers like amino acids
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21
Q

What does alpha and beta glucose look like?

A
  • Both 6 membered rings that are 3D
  • Beta glucose - C1 has OH projecting upwards the plane of the ring and H below
  • In alpha glucose this is swapped
  • MAKE SURE CARBONS BOND TO OXYGEN

https://www.google.com/search?client=firefox-b-d&sca_esv=9029f727d4831701&sxsrf=ADLYWIJBqG5mfsWfUdrzKVjKkT_YX5KLFw:1735031733791&q=alpha+and+beta+glucose+image&source=lnms&fbs=AEQNm0Aa4sjWe7Rqy32pFwRj0UkWd8nbOJfsBGGB5IQQO6L3J9LTkYkTMsFy3KExiuH6ofO9k4fklbg-dHv8qWa0fUb_IEpmKB_J5k3JZ4VHAi6k-J_thFZJG2-2F6xUFgCIEnWBSj_pmyEN9ji0rStsGqpfFchAyeHbU0WywiSnKP68Oet2MiyifXV50_DlPzhATeZVNIks&sa=X&ved=2ahUKEwjDqqrxiMCKAxW_Q0EAHbXNONAQ0pQJegQICBAB&biw=766&bih=776&dpr=1.25

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22
Q

What type of bond does a condensation reaction between 2 monosaccharides form

A

Glycosidic bonds

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23
Q

what are the 3 disaccharides

A

Maltose
Sucrose
Lactose

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24
Q

what 2 monosaccharides form maltose

A

alpha glucose + alpha glucose

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25
Q

what 2 monosaccharides form sucrose

A

glucose + fructose

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26
Q

what 2 monosaccharides form lactose

A

beta glucose + galactose

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27
Q

What are the 3 characteristics of disaccharides

A
  • Water soluble
  • Can be crystallised
  • Sweet taste
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28
Q

how do you name the bond formed in maltose

A

a - 1,4 glycosidic bond
(numbers come from the carbon number that forms the bond)

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29
Q

which of the disaccharides are reducing sugars? which are non reducing?

A

Reducing = maltose and lactose
Non reducing = sucrose

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30
Q

what are reducing sugars

A

Sugars that have a free aldehyde or ketone group (free carbonyl group)

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31
Q

What structure do you look for to determine if a sugar is reducing

A

HO - C - O - C

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32
Q

What are polysaccharides

A

molecules formed by the condensation of many glucose units which are joined by glycosidic bonds

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33
Q

what are the 3 polysaccharides

A

starch
glycogen
cellulose

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34
Q

which of the polysaccharides are formed by alpha glucose and which are made of beta

A

alpha - glyogen + starch
beta - cellulose

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35
Q

what are the 6 characteristics of polysaccharides

A
  • insoluble in water
  • compact
  • easily hydrolised
  • large molecules
  • cannot be crystallised
  • not sweet tasting
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36
Q

why is it important that polysaccharides are insoluble in water

A

so that they don’t affect the osmotic pressure of the cell

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37
Q

why is it important that polysaccharides are compact

A

means lots of energy can be stored per unit volume

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38
Q

why is it important that polysaccharides are easily hydrolised

A

they can be broken down into glucose for respiration fast

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39
Q

why is it important that polysaccharides are large molecules

A

means they cannot cross the cell membrane

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40
Q

what is starch used for

A

the major storage form of carbohydrates in plants

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41
Q

what are the 2 forms of starch

A

amylose
amylopectin (more common)

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42
Q

which of the starch forms are branched and helical

A

amylopectin

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43
Q

which of the starch forms is unbranched and helical

A

amylose

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44
Q

what is the bond formed between monomers in amylose

A

a - 1,4 glycosidic bonds

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45
Q

why does amylose coil into helices

A

because of the angle of the bonds between glucose molecules

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46
Q

what are the bonds formed in amylopectin (branched and unbranched region)

A

branched: a - 1,6 glycosidic bonds
unbranched: a - 1,4 glycosidic bonds

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47
Q

what is glycogen used for

A

major storage form of carbohydrates in animals

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48
Q

where is glycogen mostly found

A

liver and muscles - where high metabolic activities take place

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49
Q

is glycogen branched?

A

yes, more than amylopectin

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50
Q

what are the bonds formed in glycogen (branched and unbranched)

A

branched: a - 1,6 glycosidic bonds
unbranched: a - 1,4 glycosidic bonds

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51
Q

why is it important for glycogen to be branched

A

more ends for faster hydrolysis

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52
Q

what is cellulose used for

A

an important structual material in plants

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53
Q

what bonds form in cellulose

A

b - 1, 4 glycosidic bonds

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54
Q

how is cellulose able to form b - 1,4 glycosidic bonds

A

CH2OH alternataes being above and below the plane of the ring

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55
Q

is cellulose branched?

56
Q

is cellulose helical

57
Q

what bonds hold parallel cellulose molecules together

58
Q

what is a bundle of bonded cellulose molecules called

A

microfibrils

59
Q

why is the bonding of parallel cellulose molecules important

A

provides strength

60
Q

What is the food test for reducing sugars

A

benedicts test

61
Q

what is the colour range produced from the benedicts test

A

starts as blue, turns to:
green, yellow, orange, brick red

62
Q

what type of dilution is used to prepare the glucose concentrations in the benedicts test

A

serial dilution

63
Q

how do you obtain quantative results for the benedict test

A
  • use a colourimeter to find the absorbance of colour
  • Draw a graph where x axis = glucose concentration and y axis = absorbance % and draw a line of best fit
  • calibrate the curve down to the concentration

OR

Filter, dry and weigh the mass of the precipitate

64
Q

How do you test for non reducing sugars

A
  • heat with acid and neutralise
  • heat with benedicts solution
  • If a red precipitate is formed, its a non reducing sugar
65
Q

why do non reducing sugars have to be heated with acid before benedicts solution

A

to break them down into monosaccharides

66
Q

can reducing or non reducing sugars donate electrons

67
Q

what are lipids soluble / insoluble in?

A

soluble in organic solvevnts like ether
insoluble in water

68
Q

what type of relationship do lipids have with water

A

they’re hydrophobic

69
Q

are lipids polymers

70
Q

what are the 2 main groups of lipids

A

triglycerides
phospholipids

71
Q

what do trigylcerides form

A

fats and oils

72
Q

what do phospholipids form

73
Q

what molecules form trigylcerides when a condensation reaction occurs

A

one glycerol
three fatty acids

74
Q

what bonds form between glycerol and fatty acids

A

ester bonds

75
Q

what is the formation of ester bonds called

A

esterification

76
Q

what does a trigylercide look like

A

O
||
H - C - O - C - R

X 3

77
Q

what breaks down trigylcerides through hydrolysis

A

enzyme lipase

78
Q

what is glycerol

A

a chain of 3 carbons, with each carbon bonded to hydrogen and a hydroxyl group (OH)

79
Q

what does glycerol look like

A

H
|
H - C - OH
|
H - C - OH
|
H - C - OH
|
H

https://www.google.com/search?q=glycerol+molecu.e+image&client=firefox-b-d&sca_esv=c18f51794bf9b69f&sxsrf=ADLYWILnyZHA1JhjYgMZcm7vT9tA6b3hOg%3A1735059660508&ei=zOhqZ6nZHozXhbIP08LZiQc&ved=0ahUKEwip7-n18MCKAxWMa0EAHVNhNnEQ4dUDCBA&uact=5&oq=glycerol+molecu.e+image&gs_lp=Egxnd3Mtd2l6LXNlcnAiF2dseWNlcm9sIG1vbGVjdS5lIGltYWdlMgcQABiABBgNMgYQABgWGB4yCxAAGIAEGIYDGIoFMgsQABiABBiGAxiKBTIIEAAYgAQYogQyCBAAGIAEGKIEMggQABiABBiiBDIIEAAYgAQYogRI7BdQ5QRYnBZwAngBkAEAmAGMAaABrAWqAQM1LjK4AQPIAQD4AQGYAgmgAu8FwgIKEAAYsAMY1gQYR8ICDRAAGIAEGLADGEMYigXCAgkQABiABBgKGA3CAgYQABgNGB6YAwDiAwUSATEgQIgGAZAGCpIHAzYuM6AHxTE&sclient=gws-wiz-serp

80
Q

what is the structure of a fatty acid?

A
  • long carbon skeleton (a hydrocarbon chain
  • carbon at one end is a part of a
    O
    ||
    carboxyl functional group (C-O-H)
81
Q

what type of bond does the carboxyl group form with the hydrocarbon chain

A

non polar C-H bonds

82
Q

which part of the fatty acid is hydrophobic (polar) and which is hydrophylic (non-polar)

A

hydrophobic - hydrocarbon chain
hydrophylic - carboxyl group

83
Q

what makes a fatty acid saturated

A

only single covalent bonds between carbon atoms (no double bonds)

84
Q

what makes saturated lipids fat solid at room temperature

A

they lack double bonds so their flexibility allows the fat molecules to pack tightly together

85
Q

what causes unsaturated fats to be liquid at room temp

A

the double bonds cause kinks iin the fatty acid hydrocarbon chains, so they cannot pack close together

86
Q

define monosaturated

A

one double bond

87
Q

define polyunsaturated

A

more than one double bond

88
Q

what are saturated fatty acids usually found as? unsaturated?

A

saturated - animal fats
unsaturated - plant and fish oil

89
Q

describe the structure of phospholipids

A

2 fatty acids bonded to one glycerol and a phosphate group

90
Q

what type of charge does the phosphate group carry in phospholipids

91
Q

which parts of the phospholipid are hydrophobic (polar) and hydrophylic (non polar)

A

hydrophobic - hydrocarbon tails
hydrophylic - phosphate group heads

92
Q

what are 5 roles of lipids

A
  • energy storage (they store more energy than sugars)
  • component of the cell membrane
  • buoyancy
  • insulation / protection
  • they transport fat-soluble vitamins
93
Q

what tests for fats

A

emulsion test

94
Q

describe the emulsion test

A
  • add ethanold then add water and mix
  • if positive a milky emulsion will form
95
Q

what is the structure of an amino acid

A

amino group
variable group
carboxyl group

H R O
| | ||
N - C - C
| | |
H H O - H

96
Q

how many types of amino acids are there

97
Q

what bond forms when a dipeptide is made

A

peptide bond

98
Q

where does the peptide bond form in dipeptides

A

between the carboxyl group of 1 amino acid and the amino group of another amino acid

99
Q

what is a polypeptide chain

A

a chain of amino acids.

100
Q

what is a polypeptides backbond

A

the repeated N-C-C sequence

101
Q

what dimension are proteins

102
Q

what are the four protein levels

A

primary, secondary, tertiary and quaternary

103
Q

describe the primary structure of a protein

A
  • a sequence of amino acids in 1 polypeptide chain
  • determines the following structures due to the chemical nature of its backbond and side groups affecting bonding
  • a slight change in the sequence can cause the whole protein to change (mutations)
  • identifies all the amino acids present
104
Q

what are the 2 types of secondary structures

A

alpha helix and beta pleated sheets

105
Q

describe the secondary structure of a protein

A
  • coiled / pleated structure of a polypeptide chain which is held together by hydrogen bonds between the polypeptide backbone
106
Q

what causes hydrogen bonds to form in a secondary protein structure

A

within the backbone, the oxygen that is double bonded to carbon (C=O) has a partial negative charge and the hydrogen bonded to nitrogen (N-H) has a partial positive charge, causing hydrogen bonds to form

107
Q

are the hydrogen bonds in proteins secondary structure strong

A

individually no, by lots of them allow the shape to be supported

108
Q

describe the tertiary structure of a protein

A
  • further folding and coiling of both forms of the secondary structures into a 3D shape (one polypeptide) due to the interactions between the variable groups.
109
Q

what bonds form in the tertiary structure of a protein

A

hydrogen bonds
disulfide bonds
ionic bonds

110
Q

how does a disulfide bond form in tertiary protein structures

A

a covalent bond between the sulphur atoms in 2 amino acid cysteine groups (S-S)

111
Q

how do ionic bonds form in a proteins tertiary structure

A

between the carboxyl and amino grpips on the variable groups, these are ionised

112
Q

why can proteins have the same number and type of amino acids but different tertiary structures

A

different amino acid sequence
Formation of ionic or hydrogen or disulfide bonds in different places

113
Q

describe the quaternary structure of a protein

A

two or more polypeptide chains interacting

114
Q

how do you test for proteins

A

add biuret reagent (blue)
a positive result will turn puprle

115
Q

what are 4 functions of proteins

A
  • Nutrition (they form digestive enzymes)
  • Immunity
  • Growth
  • Support and movement
116
Q

what is an enzyme

A

a protein that acts as a biological catalyst which increases the rate of reaction by lowing the activation energy. they are specific to the substrate

117
Q

what causes enzymes to lower activation energys

A

They bend bonds which weakens them

118
Q

describe an active site

A
  • the location within an enzyme where a substrate is held during the chemical reaction
  • formed by only a few of the enzymes amino acids
119
Q

what is formed when an enzume and substrate bind

A

enzyme-substarte complex

120
Q

what are the two theories regarding how enzymes work

A

lock and key
induced fit

121
Q

what are the main ideas of the lock and key model

A

substrate is exactly complementary to the enzymes active sit and so the enzyme is rigid and does not change shape

122
Q

what are the main ideas of the induced fit model

A

enzymes active site and substrate are not exactly complementary, so the active shape changes shape slightly so that it is exactly complementary to the substrate, then changes back to original conformation after

123
Q

what are the 5 factors that affect the rate of enzyme reactions

A
  • enzyme concentration
  • substrate concentration
  • temperature
  • pH
  • inhibitors
124
Q

what causes enzyme reactions to meet its maximum if enzyme concentration is increasing

A

if substrate concentration is limited

125
Q

why do high temps denature enzymes

A

they cause the weak hydrogen, ionic and disulfide bonds to break which changes the enzymes active site shape, so substrates can no longer bind

126
Q

why are enzymes only functional over a narrow pH range

A

because the change in H+ ions dirsupts the ionic and hydrogen bonds in the enzyme

127
Q

what is an example of an enzyme inside and outside the cell

A

inside - lysozyme
outside - amylase

128
Q

what is an inhibitor

A

a substance that interacts with the enzyme to prevent it from working in its normal way, which stops or slows specific enzyme reactions

129
Q

what are the 2 types of inhibition, are they reversible

A

competitive and non competitive, yes

130
Q

name an irreversible inhibitor

131
Q

describe reversible inhibition

A
  • occurs when an inhibitor forms weak chemical bonds with the enzyme
  • temporary, no permanent damage to the enzyme
  • removal of the inhibitor restores normal enzyme activity
  • can be competitive or non competitive
132
Q

describe competitive inhibition (4)

A
  • inhibitor competes with the normal substrate to bind to the active site
  • usually structurally similar to the normal substrate, so fits the active site
  • prevents other substrates from binding to the active site, so decreases the rate of reaction
  • increasing the substrate concentration reverses the effect of competetive inhibitors
133
Q

what is the site where non competitive inhibitors bind to

A

the allosteric site

134
Q

describe non competitive inhibition (4)

A
  • inhibitor binds to the allosteric site
  • alters the active sites shape, so it cannot bind with the substrate
  • don’t have a similar structure to the substrate
  • effects cannot be reversed by increasing substrate concentration
135
Q

where are non competitive inhibitors typically found

A

as metabolic substances that regulate enzyme activity

Biology (7 decks)

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