biological molecules part 1 Flashcards

1
Q

what is a fancy name for a carbohydrate group

A

saccharide

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2
Q

what is a monomer

A

single molecules

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3
Q

what is a polymer

A

more than one monomer joined tog

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4
Q

what are monosaccharides

A

monomers

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5
Q

what does monosaccharides contain

A

Carbon
Hydrogen
Oxygen

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6
Q

what is the chemical formula of monosaccharides

A

(CH 0)
2 n

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7
Q

what is the function of monosaccharides

A

building blocks for larger mols

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8
Q

mono with 3 carbon name

A

triose

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9
Q

mono with 4 carbon name

A

tetrose

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10
Q

mono with 5 carbon name

A

pentose

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11
Q

mono with 6 carbon name

A

hexose

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12
Q

mono with 7 carbon name

A

heptose

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13
Q

what is the example of triose

A

glyceraldehyde

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14
Q

what is glyceraldehyde

A

used as intermediate during resperation reaction to release energy

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15
Q

what is the glyceraldehyde formula looking

A

3 C’s

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16
Q

what pentose sugar is in RNA

A

ribose

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17
Q

what pentose sugar is in DNA

A

deoxyribose

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18
Q

how to recognise ribose

A

has 2 OH

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19
Q

how to recognise deoxyribose

A

has 1 OH

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20
Q

what are the 3 monosaccharides you have to learn

A

glucose
fructose
galactose

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21
Q

what is the disaccharide formula

A

C H O
12 22 11

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22
Q

what is maltose made of

A

alpha glucose + alpha glucose

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23
Q

what is sucrose made of

A

alpha glucose + fructose

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24
Q

what is lactose made of

A

alpha glucose + galactose

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25
Q

what bonding is maltose

A

alpha 1 - 4 glycosidic bond

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26
Q

what bonding is sucrose

A

alpha 1-4 glycosidic bond

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27
Q

what bond is in lactose

A

beta 1-4 glycosidic bond

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28
Q

what reaction bonds 2 monosaccharides together

A

condensation reaction

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29
Q

condensation reaction defenition

A

bond that releases a molecule of water

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30
Q

defenition of polysaccharides

A

long chains of monosaccharides joined together by glycosidic bonds

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31
Q

what is cellulose

A

structural component of plant cell walls

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32
Q

what is startch

A

storage mol in plants

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33
Q

what is glycogen

A

storage mol in animals

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34
Q

what bonds are in cellulose

A

beta 1-4 glycosidic bonds

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35
Q

structure of amylose

A

straight chain of alpha 1-4

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36
Q

structure of amylopectin

A

branched 1-4 and 1-6

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37
Q

structure of glycogen

A

alpha branched 1-4 and 1-6

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38
Q

function of cellulose

A

strenght + support

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39
Q

how does structure of cellulose relate to function

A

straight chains = strong and rigid

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40
Q

function of startch

A

storage of glucose in plants

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41
Q

how does startch structure relate to function

A

fits in smaller spaces

insoluble so doesnt effect osmosis

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42
Q

function of glycogen

A

storage of glucose in animals

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43
Q

how does glycogen structure relate to function

A

branches - fits in a smaller space / area

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44
Q

what are oligosaccharides

A

3-9 monomers joined tog

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45
Q

what is glycogenesis

A

glucose makes glycogen

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46
Q

how to recognise fructose

A

extra CH2OH because fructose is fancy

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47
Q

how to recognise galactose

A

OH group at the top (on normal glucose its at the bottom)

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48
Q

what are the components of lipids

A

fatty acids + glycerol

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49
Q

what are the 4 roles of lipids?

A

source of energy
waterproofing
protection
insulation

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50
Q

what is the significance of lipids and waterproofing?

A

insoluble in water - preserves water

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51
Q

what is the significance of lipids and protection

A

stored around delicate organs such as kidney

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52
Q

what is the significance of lipids and insulation

A

slow conductors of heat - store body heat

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53
Q

what is an example of an insulation that lipids do?

A

electrical insulation

54
Q

electrical insulation in lipids

A

myelin sheath around nerve cells

55
Q

what is the significance of lipids and source of energy

A

when oxidised provides x2 energy comparded to carbohydrates

56
Q

what are hydrophobic

A

cannot interact with water

57
Q

what are hydrophilic

A

can interact with water

58
Q

what is in lipids

A

C H O

59
Q

solubility of lipids

A

insoluble in water

60
Q

what are triglycerides made of?

A

glycerol
3 fatty acids

61
Q

bonds in lipids

A

ester bonds

62
Q

what do all fatty acids have at end of fatty acid chain

A

carboxyl group

63
Q

what is a saturated lipid?

A

middle line (C) has no double bond

64
Q

what is a monounsaturated lipid

A

middle line (C) has one double bond

65
Q

what is a polyunsaturated lipid

A

middle line (C) has more than one double bond

66
Q

whats in a phospholipid

A

phosphate head
glycerol
2 fatty acid tails

67
Q

what bit of phospholipid is hydrophobic?

A

head

68
Q

what bit of phospholipid is hydrophiliic?

A

tail

69
Q

where are phospholipids

A

in cell membrane

70
Q

which way does the hydrophilic heads face

A

out to water

71
Q

what way does hydrophobic tail point

A

inwards

72
Q

what are steriods

A

signalling mols

73
Q

structure of steroids

A

4 carbon rings

74
Q

where are steroids found?

A

cell surface membranes

75
Q

whats the example of steroid we need to learn

A

cholesterol

76
Q

how many different types of amino acids are there?

A

20

77
Q

5 bits of a protien

A

amino group
central C
H
R group
Carboxyl group

78
Q

what bonds do proteins have

A

peptide

79
Q

what does the way the polypeptide bends depend on

A

R groups as Rs are attracted to each other

80
Q

what are primary structure determined by

A

DNA sequence of the gene which encodes the polypeptide

81
Q

why is the shape of proetin important

A

critical for its function

82
Q

what is the primary structre

A

order of amino acids in a polypeptide

83
Q

what causes the primary structure to twist into a secondary

A

hydrogen bonds

84
Q

what are the 2 types of secondary structures

A

beta plated aheet
alpha helix

85
Q

what is the tertiary structure

A

final 3d shape of polypeptide chain

critical for how proteins function

86
Q

what are quaternary

A

made of 2 or more tertiary proteins joined tog

87
Q

what shape is globular

A

spherical shape

88
Q

are globular proteins soluble in water

A

yes

89
Q

what do globular proteins have on their surface?

A

hydrophilic amino acids

90
Q

examples of globular proteins

A

haemoglobin
enzymes

91
Q

strenght of fibrous proteins

A

high tensile strenght

92
Q

solubility of fibrous proteins

A

insoluble in water

93
Q

what are on the surface of fibrous proteins

A

hydrophonic R groups

94
Q

exaples of fibrous protiens

A

collagen
keratin

95
Q

what type of mol is enzymes

A

tertiary globular proteins

96
Q

defenition of an enzyme

A

biological catalysts that speed biochemical reactions in living organisms

97
Q

4 examples of enzymes

A

carbohydrase
lipase
amylase
DNA helicase

98
Q

what would happen without enzymes

A

toxins would soon build up and the supply of respiratory substrate would decrease

99
Q

what is collision theory

A

collisions with too little energy will not produce a reaction (enzymes)

100
Q

collision theory - what does rate of reaction depends on

A

rate of succesful collisions

101
Q

is activation energy lower with or without enzyme

A

with enzyme

102
Q

relationship between enzyme and activation energy

A

enzymes increase rate of reaction by lowering activation energy

103
Q

what is the basis of lock and key model

A

shape of active sites of enzymes are exactly complementary to the shape of the substrate

104
Q

whats the new version of lock and key

A

induced fit model

105
Q

description of induced fit model

A

active site not exactly complementary but change shape in presence of specific substrate to become complementary

106
Q

whats the name of the thing that forms in enzymes

A

enzyme-substrate complex

107
Q

in induced fit what happens after enzyme substrate complex forms

A

enzyme products complex

108
Q

where can enzymes act

A

inside the cell - intracellular

outside the cell - extracellular

109
Q

what happens at 25 degrees in enzymes

A
  • low temp , kinetic energy low
  • enzyme and substrate molecules move slowly resulting in less enzyme - substrate complexes
109
Q

what does an increase in temp do in enzymes

A

greater kinetic energy

110
Q

what happens at 37 degrees in enzymes

A

higher temp, higher kinetic energy
-enzyme and substrate move quicker resulting in more enzyme substrate complexes

111
Q

what happens at 60 degrees in enzymes

A

too high temp breaks hydrogen bonds in active site changing its shape
active site no longer correspondes to substrate shape
enzymes become denatured

112
Q

what do small changes in ph in enzymes do

A

reversible changes

113
Q

what do large changes in ph in enzymes do

A

denature an enzyme

114
Q

how can enzymes be denatured

A

high temperatures
extreme pH change

115
Q

how does extreme pH change effect enzymes

A

charge on active site must attract substrate mol
if theres too much H+ (acidic) or OH- ions (alkaline)
the substrate may end up with the ame charge and repel each other

116
Q

enzyme concentration and substrate conc

A

if enzyme conc remains constant, rate of reaction will increase at the substrate concentration increases

117
Q

effect of substrate conc on enzyme activty

A

increases rate of reaction as more substrate mols present - more succesful collisions

118
Q

effect of enzyme concentration on enzyme activity

A

increasing enzyme concentration incrases the number of active sites available and therefore increase succesful collisions

119
Q

what are the types of inhibitors

A

compeitive
non competitive

120
Q

what does an inhibitor do

A

any substance which decreases the rate of enzyme catalysed reaction or stops it

121
Q

what is the name of the thing when enzyme and inhibitor form togteher

A

enzyme inhibitor complex

122
Q

what are competitive inhibitors

A

structurually similar to substrate mol so it can fit into the active site

123
Q

what do competitive inhibitors do

A

prevents enzyme substrate complexes forming

124
Q

where do non compeitive inhibitors bind to

A

anywhere else that isnt the active site

125
Q

what do non compeitive inhibitors do

A

changes the shape of the active site so the enzyme cant fit in anymore

126
Q

generally are compeitive inhibitors reversible

A

yes

127
Q

generally are non compeitive inhibitors reversible

A

no

128
Q

main differnece in compeitive vs non competiitve inhibitors

A

compeitive binds to active site

non compeitive binds to another part

129
Q

effect of increasing substrate conc on compeitive inhibitor

A

decreases inhibitor because they both compete for active site