biological molecules Flashcards

(98 cards)

1
Q

what elements do carbohydrates contain 3

A
  1. carbon
  2. hydrogen
  3. oxygen
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2
Q

what elements do lipids contain 3

A
  1. carbon
  2. hydrogen
  3. oxygen
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3
Q

what elements do proteins contain 4

A
  1. carbon
  2. hydrogen
  3. oxygen
  4. nitrogen
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4
Q

what elements do nucleic acids contain 5

A
  1. carbon
  2. hydrogen
  3. oxygen
  4. nitrogen
  5. phosphorus
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5
Q

define monomer

A

smaller units that combine to make a large molecule

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6
Q

define polymer 2

A
  1. large molecule made up of many repeating units of monomers joined together by chemical bonds
  2. process is called polymerisation
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7
Q

whats the monomer and polymer of carbohydrates 2

A
  1. monomer= monosaccharides
  2. polymer= polysaccharides
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8
Q

whats the monomer and polymer of proteins 2

A
  1. monomer= amino acids
  2. polymer= polypeptides
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9
Q

whats the monomer and polymer of nucleic acids 2

A
  1. monomer= nucleotides
  2. polymer= polynucleotides
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10
Q

define condensation

A

removal of water to form a chemical bond between 2 molecules

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11
Q

define hydrolysis

A

addition of water to break a chemical bond between 2 molecules

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12
Q

functions of carbohydrates in living organisms 5

A
  1. energy supply for cells= main role of carbohydrates
  2. energy storage= sugars can be stored as complex carbohydrates (starch/glycogen)
  3. structural components= cellulose and chitin are used in cell walls
  4. cellular recognition= glycoproteins help cells identify each other and communicate
  5. building blocks for bio molecules= deoxyribose and ribose can be used to make nucleic acids
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13
Q

explain monosaccharides 3

A
  1. subunits= one monomer
  2. examples= glucose, fructose, galactose
  3. function= energy source
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14
Q

explain disaccharides 3

A
  1. subunit = 2 dimer
  2. examples= maltose, sucrose, lactose
  3. function= transport form
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15
Q

explain polysaccharides 3

A
  1. subunit= polymer
  2. examples= starch, glycogen, cellulose
  3. function= storage form
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16
Q

explain monosaccharides 3

A
  1. simplest form of carbohydrates, also known as ‘simple sugars’
  2. soluble, sweet-tasting and found in many foods such as fruits, veg and grains
  3. general formula is (CH2O)n, n is any number from 3-7
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17
Q

what are pentose sugars

A

5 carbon atoms

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18
Q

2 examples of pentose sugars

A
  1. ribose
  2. deoxyribose
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19
Q

what are hexose sugars

A

6 carbon atoms

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20
Q

3 examples of hexose sugars

A
  1. glucose
  2. fructose
  3. galactose
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21
Q

what are the 2 isomers of glucose and what’s the difference between them

A
  1. alpha-glucose
  2. beta-glucose
  3. orientation of the hydroxyl group (OH) on carbon 1 (first carbon atom in the ring)
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22
Q

features of glucose that help it function as an energy source 2

A
  1. its soluble= hydroxyl groups can form hydrogen bonds with water, so it can be transported around organisms
  2. its bonds store lots of energy= energy released when the bonds are broken
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23
Q

what’s disaccharides

A

formed when 2 monosaccharides are joined

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24
Q

whats the 3 examples of disaccharides

A
  1. maltose (found in grains and cereals)
  2. sucrose (transport use in plants)
  3. lactose (main carb found in milk)
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25
whats maltose
glucose joined to glucose
26
whats sucrose
glucose joined to fructose
27
whats lactose
glucose joined to galactose
28
what are disaccharides
1. created via condensation reactions, and broken down via hydrolysis reactions 2. these reactions involve formation or breakdown of a covalent bond known as a glycosidic bond
29
whats a condensation reaction 2
1. when 2 monosaccharides join, a hydroxyl group (OH) of one monosaccharide reacts with a hydroxyl group (OH) of another monosaccharide 2. this forms a glycosidic bond, and a water molecule is released
30
whats a hydrolysis reaction
water molecule is added to a disaccharide, the glycosidic bond is broken to release the 2 monosaccharides
31
what are polysaccharides
complex carbohydrates made up of many monosaccharides joined via glycosidic bonds
32
examples of polysaccharides 3
1. starch, branch and unbranched 2. cellulose 3. glycogen
33
whats starch 4
1. example of a polysaccharide used by plants to store excess glucose 2. this means that starch can be hydrolysed back into glucose when plants require energy 3. starch is made of many alpha-glucose monomers joined via 1-4 and 1-6 glycosidic bonds to form chains 4. these chains come in 2 forms = branched and unbranched
34
features of starch that allow it to work well as a store of energy 5
1. insoluble= doesnt affect the water potential of the cell, so water isnt drawn in by osmosis 2. large = cant diffuse out of cells 3. many side branches= allow enzymes to hydrolyse the glycosidic bonds easily to rapidly release glucose 4. coiled= makes it compact so that a lot of glucose can be stored in a small space 5. hydrolysis releases alpha-glucose monomers= readily used in respiration
35
whats glycogen 3
1. example of a polysaccharide used by animals to store excess glucose. this means that glycogen can be hydrolysed back into glucose when animals require energy 2. glycogen is very similar to starch but used by animals instead of plants 3. made up of many alpha-glucose monomers joined via 1-4 and 1-6 glycosidic bonds to form highly branched chains
36
features of glycogen that allow it to function as a store of energy 5
1. insoluble= doesnt affect water potential of cells, water doesnt enter cells by osmosis 2. compact= a lot of glucose can be stored in a small space 3. more highly branched than starch= enzymes can easily hydrolyse the glycosidic bonds to rapidly release glucose 4. large= cant diffuse out of cells 5. hydrolysis releases alpha-glucose monomers= these are readily used in respiration
37
what's cellulose 2
1. polysaccharide formed from beta-glucose 2. primary use is to provide structural support for plant cell walls
38
explain the cellulose chemical structure 3
1. cellulose is made up of many beta glucose monomers joined together via glyosidic bonds 2. however, if 2 beta-glucose monomers line up next to each other, the hydroxyl groups on carbon 1 and carbon 4 are too far from each other to react 3. to fix this, every other beta-glucose molecule is inverted by 180 degrees (flipped upside down). this brings the hydroxyl groups close enough together to react
39
explain why many beta-glucose monomers joined together form long straight unbranched chains 2
1. the alternating inversion of the beta glucose molecules also allows for hydrogen bonds to form between individual chains 2. altho each hydrogen bond itself is relatively weak, the huge no of these bonds provides great strength to cellulose as a whole
40
cellulose chains, microfibrils and macrofibrils /2/
1. multiple cellulose chains become tightly cross linked via hydrogen bonds to form bundles called microfibrils 2. these microfibrils join together to make macrofibrils which combine to make strong cellulose fibres in the plant cell wall
41
adaptations of cellulose for its role 3
1. long, straight and unbranched chains= provide rigidity to the cell wall 2. hydrogen bonds= cross link the chains to add collective tensile strength 3. microfibrils= provide additional strength
42
what are the 2 groups of all sugars
1. reducing sugars= all monosaccharides and some disaccharides such as maltose/lactose 2. non reducing sugars= some disaccharides such as sucrose and all polysaccharides
43
steps for seeing if the sample is a reducing sugar /4/
1. place 2cm^3 of ur sample into a test tube 2. add an equal volume of benedict's reagent 3. heat the mixture in a gently boiling water bath for 5 mins 4. if a reducing sugar is present, the solution goes from a blue solution to a red precipitate
44
how to determine the concentration of reducing sugar present in the sample 4
1. blue = no reducing sugar is present 2. green = low concentration 3. orange = a medium conc 4. brick-red = high conc
45
quantitative methods to determine the conc of reducing sugar /2/
1. use a colorimeter to measure the absorbance of each solution 2. filter the solution and weigh the precipitate
46
testing for non-reducing sugars 2
1. NRS give a negative result for the normal reducing sugars test 2. to test for these, you must first hydrolyse them into their monosaccharide components
47
stages for testing for non-reducing sugars 6
1. negative result for reducing sugars test 2. add 2cm^3 of the food sample to 2cm^3 of dilute hydrochloric acid 3. heat the mixture in a gently boiling water bath for 5 mins (acid hydrolyses disaccharides into monosaccharides 4. neutralise this mixture by adding sodium hydrogencarbonate solution 5. retest this mixture using the test for reducing sugars 6. if non-reducing sugars were present at the start, the mixture will change from a blue solution to a brick red precipitate
48
steps to test for starch 3
1. place 2cm^3 of ur food sample into a test tube 2. add a couple drops of iodine solution and shake 3. if starch is present, the solution goes from orange to blue-black
49
what are lipids 2
1. biological molecules that contain the elements: carbon, hydrogen, oxygen. lower proportion of oxygen than carbohydrates 2. not made of a long chain of monomers so their not considered polymers
50
functions of lipids 5
1. energy supply= lipids can be oxidised to provide energy for cells 2. structural components= phospholipids are used in cell membranes 3. water-proofing= insoluble lipids are used to form water-resistant barriers 4. insulation= lipids can help retain heat or act as electrical insulators 5. protection= delicate organs are surrounded by a layer of fat
51
fatty acids 2
1. most lipids are made up of fatty acids combined with an alcohol (usually glycerol) 2. fatty acids consist of a carboxyl group attached to a hydrocarbon chain (R group)
52
what are saturated fatty acids 3
1. have hydrocarbon chains that are 'saturated' with hydrogen, meaning all carbon atoms are bonded to the max no of hydrogen atoms 2. hydrogen carbon has no carbon-carbon double bonds 3. lipids that contain saturated fatty acids have higher melting points and so are usually solid at room temperature
53
what are unsaturated fatty acids 3
1. have hydrocarbon chains that dont contain the max no of hydrogen atoms bonded to the carbon atoms 2. hydrocarbon chain has atleast one carbon-carbon double bond, causes the chain to kink 3. lipids that contain unsaturated fatty acids have lower melting points and so are liquids at room temp
54
what may unsatured fatty acids be 2
1. monounsaturated= one double bond 2. polyunsatured= 2 or more double bonds
55
how to test for lipids 5
1. place ur food sample in a test tube 2. add 2cm^3 of ethanol 3. shake 4. add 2cm^3 of distilled water 5. if lipids are present, a milky white emulsion appears
56
whats a triglyceride 3
1. type of lipid used as a store of energy in animals, plants and some bacteria 2. consists of a glycerol backbone attached to 3 fatty acid tails 3. each fatty acid tail contains a hydrocarbon chain (R) which can vary in length, may be saturated or unsaturated
57
features that allow triglycerides to store energy efficiently /4/
1. long hydrocarbon tails= their many carbon-hydrogen bonds can be broken to release energy 2. low mass to energy ratio= lots of energy stored in a small volume 3. insoluble= dont affect water potential of cells as their large and non-polar 4. high ratio of hydrogen to oxygen atoms= release water when oxidised
58
how are triglycerides formed thru condensation reaction 2
1. hydroxyl groups (OH) on the glycerol and on the 3 fatty acids react together to release 3 water molecules (h20) 2. results in 3 ester bonds between the glycerol and fatty acids
59
how are triglycerides broken apart thru hydrolysis reactions 2
1. addition of 3 water molecules breaks the ester bonds 2. separates the glycerol and fatty acids
60
whats a phospholipid 2
1. type of lipid used as a structural component of the cell membrane 2. similar to triglycerides except one of the fatty acid tails is replaced by a phosphate group
61
whats a phospholipid made up of 2
1. hydrophilic head= contains glycerol and phosphate 2. hydrophobic tail= contains fatty acids
62
explain phospholipid bilayer
1. when phospholipids are placed in water, they arrange themselves into a double layer so that the hydrophilic heads are facing out (towards the water) and hydrophobic tails are facing in (away from the water) 2. creates a hydrophobic centre in the bilayer so water-soluble molecules cant pass through
63
what are proteins made up of 2
1. amino acids, which are essential macromolecules involved in various functions within living organisms 2. amino acids are monomers, can join together via peptide bonds to form dipeptides and polypeptides
64
functions of proteins in living organisms 6
1. enzymes= proteins used to breakdown and synthesise molecules 2. antibodies= proteins involved in the immune response 3. transport= some can move molecules or ions across membranes 4. structural components= keratin and collagen used to create strong fibres 5. hormones= proteins that act as chemical messengers in the body 6. muscle contraction= muscles are made of proteins
65
general structure of an amino acid 5
1. central carbon atom 2. amino group 3. carboxyl group 4. hydrogen atom 5. R group or variable side group
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how do amino acids differ 2
1. different R group which determines its properties 2. e.g= amino acid cysteine contains a sulphur atom in its R group, allows cysteine to form disulphide bonds
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how are dipeptides synthesised or broken down 2
1. dipeptides are synthesised via condensation reactions, broken down via hydrolysis reactions 2. these reactions involve the formation or breakdown of a covalent bond known as a peptide bond
68
what happens in a condensation reaction for amino acids
1. when 2 amino acids join, the hydroxyl in the carboxyl group of one amino acid reacts with the hydrogen in the amino group of another amino acid 2. this releases a water molecule and forms a peptide bond between the carbon of one amino acid and the nitrogen of another
69
what happens in a hydrolysis reaction for amino acids 2
1. when a water molecule is added to a dipeptide 2. the peptide bond is broken to release the 2 amino acids
70
how to test for proteins 3
1. place ur food sample in a test tube 2. add an equal volume of biuret solution (sodium hydroxide and copper sulfate) 3. if proteins are present, solution goes from blue to purple, if not it stays blue
71
primary structure of proteins 3
1. made up of the unique sequence of amino acids in the polypeptide chain 2. structure held together by peptide bonds 3. a change to just one of the amino acids can result in a change to a protein's structure and function
72
secondary structure of proteins 2
1. hydrogen bonds forming between the amino group of one amino acid and the carboxyl group of another amino acid further down the chain 2. causes the polypeptide chain to coil into either an alpha-helix or a beta-pleated sheet
73
how does the tertiary structure form
polypeptide chain folds and twists further to create a complex 3D structure
74
what bonds are involved in the tertiary structure /4/
1. hydrogen bonds= individually weak, provide strength in large numbers 2. ionic bonds= form between positive and negative R groups 3. form between R groups that contain sulfur like cysteine 4. hydrophobic and hydrophilic interactions= weak interactions between polar and non-polar R groups
75
what's the quaternary structure /2/
1. involves 2 or more polypeptide chains held together by same bonds found in tertiary structure 2. can also involve the addition of non-protein groups as prosthetic groups
76
what are enzymes /2/
1. globular proteins with complex and unique tertiary structures 2. known as catalysts, speed up the reaction without being used in the reaction
77
define activation energy /3/
1. energy required for a chemical reaction to be started 2. without sufficient activation energy, the reactant molecules wont have enough energy to break their bonds and form new ones to form the desired products 3. enzymes work by lowering the activation energy for a chemical reaction, this means reactions are able to take place at lower temperatures (e.g= body temperatures)
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what are intracellular enzymes
act within cells that produce them
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what are extracellular enzymes
act outside the cells that produce them, and are secreted
80
process of enzymes binding with substrates 4
1. enzymes have unique tertiary structures which determine the shape of their active site, shape is complementary to the substrate 2. substrate binds to the active site to form an enzyme-substrate complex 3. temporary bonds form between the R groups within the active site and substrate. these bonds lower the activation energy to help break down the substrate into products 4. the products are released from the active site, leaving the enzyme free to be used again
81
whats the lock and key model
substrate fits perfectly into the enzyme's active site
82
whats the induced fit model 3
1. substrate doesnt fit perfectly into the enzyme's active site 2. as the substrate enters the enzyme, the active site shape changes slightly 3. this puts a strain on the substrate's bonds which lowers the activation energy
83
what are the 4 factors that affect enzyme-controlled reactions
1. temperature 2. pH 3. substrate conc 4. enzyme conc
84
describe how temp affects enzyme activity
1. as temp increases, rate of reaction increases 2. max rate is reached at the optimum temp 3. as temp reaches past the optimum, rate of reaction decreases until the reaction stops
85
explain how temp affects enzyme activity 3
1. the molecules have more kinetic energy, causing more collisions and enzyme-substrate complexes 2. optimum temp is the temp the enzyme works fastest at 3. too much kinetic energy causes the active site to change shape and the enzyme denatures
86
describe how ph affects enzyme activity 3
1. below the optimum ph, the rate of reaction is low 2. max rate of reaction is reached at the optimum ph 3. above the optimum ph, the rate of reaction is low/zero
87
explain how ph affects enzyme activity 3
1. in acidic conditions, H+ ions break ionic/hydrogen bonds and denature enzymes 2. optimum ph is the ph the enzyme works fastest at 3. in alkaline conditions, OH- ions break ionic bonds/hydrogen bonds and denature enzymes
88
describe how substrate conc affects enzyme activity 2
1. as substrate conc increases, the rate of reaction increases 2. as substrate conc increases further, the rate of reaction levels off
89
explain how substrate conc affects enzyme activity 2
1. more substrate molecules to form ES complexes 2. this is the saturation point, which is when all active sites are occupied by a substrate and enzyme conc becomes the limiting factor
90
describe how enzyme conc affects enzyme activity 2
1. as the enzyme conc increases, the rate of reaction increases 2. as the enzyme conc increases further, the rate of reaction levels off
91
explain how enzyme conc affects enzyme activity 2
1. there are more enzymes to form ES complexes 2. all substrate molecules available are being acted upon and substrate conc becomes the limiting factor
92
define inhibitors
molecules that bind to enzymes to reduce their activity
93
what are the 2 effects that inhibitors can have
1. reversible= form weak bonds (hydrogen/ionic) with the enzyme 2. irreversible= form strong bonds (covalent) with the enzyme
94
what are the 2 types of inhibitors
1. competitive= bind to the active site 2. non competitive= bind away from the active site
95
explain competitive inhibitors 5
1. bind to the active site of an enzyme to prevent ES complexes 2. similar shape to the substrate and so they bind to the active site of enzyme 3. this prevents the substrate from binding, reducing formation of ES complexes 4. decreases rate of enzyme-catalysed reaction 5. most of these are reversible, temporarily bind to the active site
96
how is the effect of competitive inhibitors reduced 3
1. increasing the substrate conc 2. the higher the substrate conc the more likely it is that the substrates will bind to the active site rather than inhibitor molecules 3. reduces effect of competitive inhibitors
97
explain non-competitive inhibitors 3
1. bind to enzymes away from the active site (allosteric site) to prevent ES complexes 2. this binding changes the tertiary structure of an enzyme, causing the active site to change shape 3. results in the active site no longer complementary to the substrate so less ES complexes are formed and rate of enzyme catalysed reaction decreases
98
Increasing substrate concentration has no effect on the rate of reaction 2
1. non comp inhibitors cant be overcome by increasing substrate conc 2. they dont compete with the substrate to bind to the active site, so increasing substrate conc has no effect on the rate of reaction