Biological Molecules Flashcards

1
Q

What is a polymer

A

A long chain of monomers bonded together

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2
Q

What is a monomer

A

Small units which make large molecules

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3
Q

What are 5 molecules which help organism’s to function

A

Water , nucleic acids ( DNA & RNA ) proteins , carbohydrates , lipids

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4
Q

What are monosaccharides

A

Monomers : glucose , gulactose , ribose and fructose

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5
Q

What are disacharides

A

2 monomers joined together : lactose , maltose , sucrose

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6
Q

What are polysacharides

A

Polymers like cellulose , starch & glycogen

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7
Q

What is a condensation reaction

A

A reaction which joins chemicals while releasing water

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8
Q

What is hydrolysis

A

Using water to break a molecule into 2

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9
Q

Glucose + glucose =

A

Maltose + water

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10
Q

Glucose + gulacotse =

A

Lactose + water

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11
Q

Glucose + fructose =

A

Sucrose + water

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12
Q

What are polysaccharides - and 3 examples ?

A

Lots of monomers bonded together by a glycosydic bond in a condensation reaction E g : cellulose , starch and glycogen

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13
Q

What elements di all carbohydrates contain ?

A

Carbon , hydrogen and oxygen

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14
Q

Monomer for carbohydrates ?

A

Monosaccharides

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15
Q

Polymer for carbohydrates ?

A

Polysaccharide and disaccharide

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16
Q

Protein monomer and polymer

A

Amino acids and polypeptides and proteins

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17
Q

What ratio do hydrogen and oxygen have in carbohydrates

A

2:1

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18
Q

What bonds to carbohydrates have

A

Glycosidic bond

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19
Q

Definition and example of disaccharide

A

2 monomers bonded by a glycosidic bond through a condensation reaction . Eg : lactose , sucrose , maltose

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20
Q

2 types of hexose ?

A

Alpha glucose ( H at c1 ) and Beta glucose ( OH at c1)

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21
Q

What is a pentose

A

Carbohydrate with 5 carbons

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22
Q

2 pentose we need to know

A

Oxyribose ( includes OH at c2 ) and deoxyribose ( contains h at c2)

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23
Q

Why isnt fat classed as a monomer ?

A

It contains glycerol AND fatty acids ] not got 1 repeating unit

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24
Q

What elements do proteins contain ?

A

Carbon , hydrogen , oxygen , sulpher , nitrogen

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25
What elements do nucleic acids contain ?
Carbon , hydeogen , oxygen , nitrogen and phosphurus
26
2 glucose isomers :
Alpha glucose - H at c1 Beta - has OH at c1
27
give 2 examples of reducing sugars :
maltose and lactose
28
give 1 example of non reducing sugars
sucrose
29
2 examples of polysaccharides of starch made by alpha glucose
amylose & amylopectin
30
starch & its relationship with water
its insoluble - water cant get into cell by osmosis and cause it to swell
31
amylopectin structure
- long branched molecule of alpha glucose - glyosidic bonds between carbon 1-4 and carbon 1 -6 . - hydrolysis of glucose easily - plants
32
amylose structure
- long unbranched chain of alpha glucose - glycosydic bond between carbon 1 and 4 - twist to form helix - compact - good for energy storag-plants
33
glycogen structure
-animals - alpha glucose bonds - highly branched - hydrolysis of glucose quickly - can coil - compact - good energy storage
34
cellulose structure
-plants in cell wall - beta glucose - unbranched - c1 an c4 to far to react so alternate beta glucose molecules turn upside down to react - chains held together by hydrogen bonds - forms microfibres - good for structural support
35
what elements are lipids made of ?
carbon , hydrogen and oxygen
36
what is different between the ratio of H:O in carbohydrates than lipids ?
carbohydrates have 2 : 1 where as lipids have very few oxygens compared to hydrogens .
37
solubility of lipids ?
insoluble in water , but soluble in solvents
38
triglyceride structure :
one molecule of glycerol and three fatty acids . insoluble in water ester bond holds fatty acid to glycerol essential fatty acids complete fatty acids . condensation reaction
39
glycerol structure
has 3 hydroxyl group is an alcohol essential for making ester bond through condensation reaction
40
saturated fatty acid
- single bond saturated with hydrogen animal fats raise cholesterol level - bad fats solid at room temp
41
unsaturated fatty acids :
= double bond unsaturated chain kinks unsaturated fatty acids plant fats reduce cholesterol level - good fats liquid at room temp .
42
fatty acids structure
a methyl group (CH3) hydrocarbon chain ( R group ) carboxyl group tail of fatty acids hydrophobic - insoluble in water .
43
what are the 4 roles of lipids in organisams ?
energy source waterproofing heat / thermal energy protection
44
energy source - lipids
energy can be broken down during respiration lipids can be broken down into CO2 + H2O- produce more energy than respiration of sugar
45
waterproofing lipids
waxy cuticle ontop of leaves
46
insulation lipids
heat insulator - layer of fat under skin , slow conductor of heat thermal energy
47
protection lipids
fat can be found around delicate organs
48
lipids - structure related to properties : tryglicerides
excellent source of energy - many hydrogen to carbon bonds good storage molecules - lots of energy can be stored in small volume no effect on water potential as triglycerides are hydrophobic source of water molecules as oxidation of hydrocarbon bonds release quickly desert animals retain if no liquid water to drink .
49
phospholipids structure :
2 fatty acids - hydrophobic - hates water 1 glycerol molecule i phosphate molecule - hydrophilic - attract to water
50
what happens when phospholipid is placed in water
heads are hydrophilic so faces water tails ae hydrophobic so faces away from water as possible .
51
what bonds do polypeptides form ?
peptide bonds
52
dipeptide definition :
2 amino acids bonded together by a peptide bond in a condensation reaction
53
polypeptide definition :
lots of amino acids bonded together to form a peptide bond in a condensation reaction
54
where is peptide bond found ?
in-between carbon and nitrogen
55
in a condensation reaction of AA , where does the water molecule come from ?
OH from carboxyl group of 1 AA and H from the AA adjacent to that AA from the amine group
56
structure of AA
COOH - carboxyl group H2N - amine / amino group H group R group - anything additional - makes amino acid different ( variable region )
57
4 protein structures
- primary - secondary - tertiary - quaternary
58
primary structure of proteins
long chain of different amino acids held by peptide bonds - A polypeptide chain
59
secondary structure of proteins
forms alpha helix or beta plated sheet - held by hydrogen bonds these bonds are between : C from COOH , and N from NH2 and O from COOH and H from NH2
60
tertiary structure of proteins
- proteins become further folded - 3D - held in shape by : Ionic bonds , disulphide bond and hydrogen bond . I&D bonds form between r groups of different amino acids D bond sometimes occur
61
quaternary structure
more than 1 polypeptide chain working together EG haemoglobin
62
what protein structure do enzymes have
most of the time they have tertiary structure rarely they have quaternary structure
63
what is activation energy
minimum amount of energy needed for reaction to occur -energy released from the reaction should never be more than amount of energy entering the reaction
64
what pros come from lowering the activation energy
-less time - less energy - less money as less energy / time/temp is required to start reaction
65
describe structure of enzymes
- biological catalyst - globular proteins with specific 3d shape - active site is specific region of enzyme which is functional (eg through making reactions or during induced fit )
66
what do enzymes do
speed up ROR without being used up globular proteins catalyse conversion of large molecules into product molecules work inside cells( intracellular ) workoutside cells (extracellular )
67
one intracellular enzyme you need to know
catalayse
68
catalase info
- harmful to cells hydrogen peroxide is harmful to our bodies so it converts it into water and oxygen
69
2 extracellular enzymes you need to know
amylase & trypsin
70
what does amalays do ?
- hydrolysis of starch into maltose . secreted by salivary glands , pancreas
71
trypsin info
- 1st section of digestion of amino acids - breaks down long chain proteins into smaller chains of proteins . - catalyses hydrolysis of peptide bonds
72
induced fit model :
- enzyme has an active site - active site isn't complimentary to substrate - active site alters itself to become complimentary - substrate enters enzyme - forms enzyme substrate complex - strain on bonds of active site - they weaken (hydrogen bonds ) - products are produced and leave active site .
73
what 2 conditions need to be met for an enzyme to work
- enzyme must come in direct contact with substrate - have an active site which fits substrate
74
what effects enzyme action ?
- Ph - Concentration of substrate and enzyme - Temperature
75
why can changing one of the amino acid orders could prevent enzyme from functioning ?
it may change the structure of AA causing the substrate to not fit enzyme thus reaction will not work .
76
ROR for substrate
- at begging very steep line - lots of reactants are turning into products in a short space of time ( ROR increase ) - gradually decrease in reactants so ROR decreases - eventually ran out of reactants (reaction has stopped)
77
ROR for products
- initially no product - increase in amount of product as substrate is being broken down - as less substrate is broken down less product is formed - eventually no product is formed
78
ROR of straight line - how it can be measured
the gradient change in y over change in x
79
ROR of curved line - how it can be measured
draw tangent on desired point - measure change in y over change in x
80
what is the effect of temperature on ROR
- as the temp increases , the particles gain more KE - so there are more collisions , and more successful collisions - there are more ESC'S formed - Optimum temperature is the highest temp where most reactions take place - eventually the temp is so high that it breaks the weak H2 bonds - this alters shape of enzyme ( tertiary shape of enzyme ) so substrate cannot fit - reaction eventually stops
81
what is the effect of pH on ROR
- as pH increases more ESC' s form so more reactions occur . gradually nearer it gets to optimum the higher the KE - if pH is too high or to low the enzyme will denature so no ESC's can form
82
what is the effect of enzyme concentration on ROR
- at beginning -more enzyme concentration = more substrate can be converted into products - increase in enzyme conc = increase in ROR - - gradually at end if there is an increase enzyme molecules = no effect as already have enough enzymes for reaction so rate stays consent .
83
what is the effect of substrate concentration
- ROR increases in proportion to conc of sub - increase in sub = fast ROR so more ESC's form occurs till saturation point ( where rate wont change no matter how much more sub you add
84
what is a competitive inhibitor ?
an inhibitor which directly fits into active site - and temporarily occupying it - less ESC's form - an increase in conc of substrate ' knocks out the inhibitor ' so inhibitor will have no effect
85
example of competitive inhibitor
malonate - blocks succinate
86
what is a monomer for a nucleic acid
nucleotide
87
4 nitrogenous bases are
- Adenine - Cytosine - Thymine - Guanine
88
how do nucleic acids form ?
condensation reaction occurs , weak h2 bonds break , water is released , phosphodiester bond is formed between C3 and deoxyribose sugar
89
2 similarities for DNA & RNA
both contain - 4 nitrogenous bases - phosphate group
90
2 differences for RNA & DNA
DNA = A ,C ,T ,G RNA = A,C,U,G, DNA = DEOXYRIBOSE RNA = OXYRIBOSE
91
how many hydrogen bonds do A-T AND G-C form
A to T = 2 bonds C to G = 3 bonds
92
what backbone do nucleic acids contain ?
phosphodiester backbone
93
5 properties of nucleic acids
- stable becasue of bonds - large molecules - lots of info stored - weak h2 bonds = easily broken for replication - base pairs can replicate - base pair backbone = strength
94
what is the process of mitosis
- DNA replication - increase in number of sub cellular structures - cell membrane divide produce 2 identical daughter cells - growth an repair - identical cells.
95
stage 1 o DNA replicaion :
original strand of DNA - H2 bonds between bases are broken by enzyme helicase . DNA strands unwind - both strands separate .stagw
96
stage 2 of DNA replication
- hydrolysis of H2 bonds - as strands separate , remaining bases form template - free floating nucleotides align to complimentary base pair .
97
stage 3 of DNA replication
- free floating nucleotides join to exposed basis - all bonds destroyed - further hydrolysis
98
stage 4 of DNA replication
phosphodiester bonds form due to condensation reaction due to enzyme polymerase which catalyses reaction . h2 bonds form
99
stage 5 DNA replication
2 identical copies of DNA produced - replicated DNA winds back into helix shape .
100
what does ATP stand for ?
adenosine triphosphate
101
what is the structure of ATP
it has 1 adenine 1 ribose sugar 3 phosphate groups
102
what does ADP stand for ?
adenosine diphosphate
103
what is ADP structure
1 adenine 1 ribose sugar 2 phosphate groups
104
bonds found in ADP & ATP ?
phosphate bond between phosphate groups ester bond found between ribose sugar and phosphate base hydrogen bond found between base and ribose
105
what is ATP used for
releasing energy for chemical reactions
106
why is ATP more useful than ADP
ATP has a 3rd phosphate group which releases a lot of energy . when it is hydrolysed .
107
equation for ATP form
ADP + P = ATP condensation reaction
108
equation for ATP storing energy
ATP = ADP + P + energy
109
ATP synthase is for ?
making ATP
110
ATP hydrolase is for ?
releasing energy
111
synthesis of ATP
reversible reaction catalysed ATP synthase condensation reaction
112
ATP properties
- small easy to move - water soluble - bonds between phosphates - releases energy in small quantities easily generated
113
ATP is a energy rich product - how does this help ?
- helps metabolic processes - energy stored in phosphate bonds
114
water molecule properties
- dipolar ( 2 charges ) - slight +ve charge for hydrogens - slight -ve charge for Oxygen they attract weak hydrogen bonds
115
why are hydrogen bonds weaker than covalent bonds
H bonds - between molecules covalent bonds within molecules .
116
what are the 5 properties of water
metabolism solvent liquid density surface tension - light animals can walk latent heat of vaporisation high specific heat capacity - stable environment - buffering cohesion - stick together
117
metabolite meaning :
solvent ( things can dissolve in it ) so reactions can occur EG : glucose in blood
118
liquid as property meaning FOR WATER
it can flow easily . makes and breaks hydrogen bonds
119
density water properties
density increases as it goes colder till 4 degrees. after that it gets lighter . help provide insulation ( ice can form a layer on top of water ) to help with insulation .
120
solvent properties of water
ions can be dissolved as -ve charge as +ve cgarge can attract to -ve oxygen .
121
high specific heat capacity
hydrogen bonds absorb alot of energy limits rapid buffer change in temp
122
cohesion properties of water :
attraction between water molecules
123
high latent heat of vaporisation :
takes a lot of energy to break hydrogen bonds provide cooling effect - sweating when hot .
124
inorganic ions do not contain which element :
carbon
125
how do hydrogen ions affect enzyme action
pH is e4ffected by h +
126
3 inorganic ions you need to know
- iron - hydrogen - phosphate
127
sodium ion used for :
generating nerve impulses for muscle contraction eg co transport in glucose / amino acids
128
hydrogen ion used for :
affect ph of substances
129
phosphate ion used for :
photosynthesis and respiration reactions used for DNA /ATP
130
iron ion used for :
compound of haemoglobin links to transport of oxygen
131
what is definition of an isomer
a molecule with the same molecular formula but different arrangement