biological molecules part 1 Flashcards

(131 cards)

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
what bonding is maltose
alpha 1 - 4 glycosidic bond
26
what bonding is sucrose
alpha 1-4 glycosidic bond
27
what bond is in lactose
beta 1-4 glycosidic bond
28
what reaction bonds 2 monosaccharides together
condensation reaction
29
condensation reaction defenition
bond that releases a molecule of water
30
defenition of polysaccharides
long chains of monosaccharides joined together by glycosidic bonds
31
what is cellulose
structural component of plant cell walls
32
what is startch
storage mol in plants
33
what is glycogen
storage mol in animals
34
what bonds are in cellulose
beta 1-4 glycosidic bonds
35
structure of amylose
straight chain of alpha 1-4
36
structure of amylopectin
branched 1-4 and 1-6
37
structure of glycogen
alpha branched 1-4 and 1-6
38
function of cellulose
strenght + support
39
how does structure of cellulose relate to function
straight chains = strong and rigid
40
function of startch
storage of glucose in plants
41
how does startch structure relate to function
fits in smaller spaces insoluble so doesnt effect osmosis
42
function of glycogen
storage of glucose in animals
43
how does glycogen structure relate to function
branches - fits in a smaller space / area
44
what are oligosaccharides
3-9 monomers joined tog
45
what is glycogenesis
glucose makes glycogen
46
how to recognise fructose
extra CH2OH because fructose is fancy
47
how to recognise galactose
OH group at the top (on normal glucose its at the bottom)
48
what are the components of lipids
fatty acids + glycerol
49
what are the 4 roles of lipids?
piws protection insulation waterproofing source of energy
50
what is the significance of lipids and waterproofing?
insoluble in water - preserves water
51
what is the significance of lipids and protection
stored around delicate organs such as kidney
52
what is the significance of lipids and insulation
slow conductors of heat - store body heat
53
what is an example of an insulation that lipids do?
electrical insulation
54
electrical insulation in lipids
myelin sheath around nerve cells
55
what is the significance of lipids and source of energy
when oxidised provides x2 energy comparded to carbohydrates
56
what are hydrophobic
cannot interact with water
57
what are hydrophilic
can interact with water
58
what is in lipids
C H O
59
solubility of lipids
insoluble in water
60
what are triglycerides made of?
glycerol 3 fatty acids
61
bonds in lipids
ester bonds
62
what do all fatty acids have at end of fatty acid chain
carboxyl group
63
what is a saturated lipid?
middle line (C) has no double bond
64
what is a monounsaturated lipid
middle line (C) has one double bond
65
what is a polyunsaturated lipid
middle line (C) has more than one double bond
66
whats in a phospholipid
phosphate head glycerol 2 fatty acid tails
67
what bit of phospholipid is hydrophobic?
head
68
what bit of phospholipid is hydrophobic?
tail
69
where are phospholipids
in cell membrane
70
which way does the hydrophilic heads face
out to water
71
what way does hydrophobic tail point
inwards
72
what are steriods
signalling mols
73
structure of steroids
4 carbon rings
74
where are steroids found?
cell surface membranes
75
whats the example of steroid we need to learn
cholesterol
76
how many different types of amino acids are there?
20
77
5 bits of a protien
amino group central C H R group Carboxyl group
78
what bonds do proteins have
peptide
79
what does the way the polypeptide bends depend on
R groups as Rs are attracted to each other
80
what are primary structure determined by
DNA sequence of the gene which encodes the polypeptide
81
why is the shape of proetin important
critical for its function
82
what is the primary structre
order of amino acids in a polypeptide
83
what causes the primary structure to twist into a secondary
hydrogen bonds
84
what are the 2 types of secondary structures
beta plated aheet alpha helix
85
what is the tertiary structure
final 3d shape of polypeptide chain critical for how proteins function
86
what are quaternary
made of 2 or more tertiary proteins joined tog
87
what shape is globular
spherical shape
88
are globular proteins soluble in water
yes
89
what do globular proteins have on their surface?
hydrophilic amino acids
90
examples of globular proteins
haemoglobin enzymes
91
strenght of fibrous proteins
high tensile strenght
92
solubility of fibrous proteins
insoluble in water
93
what are on the surface of fibrous proteins
hydrophonic R groups
94
exaples of fibrous protiens
collagen keratin
95
what type of mol is enzymes
tertiary globular proteins
96
defenition of an enzyme
biological catalysts that speed biochemical reactions in living organisms
97
4 examples of enzymes
carbohydrase lipase amylase DNA helicase
98
what would happen without enzymes
toxins would soon build up and the supply of respiratory substrate would decrease
99
what is collision theory
collisions with too little energy will not produce a reaction (enzymes)
100
collision theory - what does rate of reaction depends on
rate of succesful collisions
101
is activation energy lower with or without enzyme
with enzyme
102
relationship between enzyme and activation energy
enzymes increase rate of reaction by lowering activation energy
103
what is the basis of lock and key model
shape of active sites of enzymes are exactly complementary to the shape of the substrate
104
whats the new version of lock and key
induced fit model
105
description of induced fit model
active site not exactly complementary but change shape in presence of specific substrate to become complementary
106
whats the name of the thing that forms in enzymes
enzyme-substrate complex
107
in induced fit what happens after enzyme substrate complex forms
enzyme products complex
108
where can enzymes act
inside the cell - intracellular outside the cell - extracellular
109
what happens at 25 degrees in enzymes
- low temp , kinetic energy low - enzyme and substrate molecules move slowly resulting in less enzyme - substrate complexes
109
what does an increase in temp do in enzymes
greater kinetic energy
110
what happens at 37 degrees in enzymes
higher temp, higher kinetic energy -enzyme and substrate move quicker resulting in more enzyme substrate complexes
111
what happens at 60 degrees in enzymes
too high temp breaks hydrogen bonds in active site changing its shape active site no longer correspondes to substrate shape enzymes become denatured
112
what do small changes in ph in enzymes do
reversible changes
113
what do large changes in ph in enzymes do
denature an enzyme
114
how can enzymes be denatured
high temperatures extreme pH change
115
how does extreme pH change effect enzymes
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
enzyme concentration and substrate conc
if enzyme conc remains constant, rate of reaction will increase at the substrate concentration increases
117
effect of substrate conc on enzyme activty
increases rate of reaction as more substrate mols present - more succesful collisions
118
effect of enzyme concentration on enzyme activity
increasing enzyme concentration incrases the number of active sites available and therefore increase succesful collisions
119
what are the types of inhibitors
compeitive non competitive
120
what does an inhibitor do
any substance which decreases the rate of enzyme catalysed reaction or stops it
121
what is the name of the thing when enzyme and inhibitor form togteher
enzyme inhibitor complex
122
what are competitive inhibitors
structurually similar to substrate mol so it can fit into the active site
123
what do competitive inhibitors do
prevents enzyme substrate complexes forming
124
where do non compeitive inhibitors bind to
anywhere else that isnt the active site
125
what do non compeitive inhibitors do
changes the shape of the active site so the enzyme cant fit in anymore
126
generally are compeitive inhibitors reversible
yes
127
generally are non compeitive inhibitors reversible
no
128
main differnece in compeitive vs non competiitve inhibitors
compeitive binds to active site non compeitive binds to another part
129
effect of increasing substrate conc on compeitive inhibitor
decreases inhibitor because they both compete for active site
131
What the monomer of protein
Amino acid