2.1.2 biological molecules Flashcards

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1
Q

covalent bonding

A

atoms share a pair of electrons, stronger bonds, between non-metals

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2
Q

ionic bonding

A

electrons are transferred from one atom to another, slightly weaker bonds, between metal and non-metal

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3
Q

hydrogen bonding

A

slightly negative region of one polar molecule and slightly positive region of another attract each other to form a weak bond but can collectively form important forces that alter physical properties of molecules

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4
Q

polymer

A

long chain molecule made up of a large number of repeating units linked together
e.g. protein, DNA, starch

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5
Q

monomer

A

small basic molecular unit that make up polymers
e.g. amino acids, nucleotides, monosaccharides

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6
Q

monomer: glucose

A

polymer: polysaccharide (amylose, amylopectin, cellulose, glycogen)

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7
Q

monomer: amino acid

A

polymer: polypeptide (protein)

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8
Q

monomer: nucleotides

A

polymer: nucleic acid (DNA, RNA)

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9
Q

all carbohydrates contain…

A

carbon
hydrogen
oxygen

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10
Q

all proteins contain…

A

carbon
hydrogen
oxygen
nitrogen
sometimes sulfur

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11
Q

all nucleic acids contain…

A

carbon
hydrogen
oxygen
nitrogen
phosphorous

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12
Q

all lipids are made of…

A

carbon
hydrogen
oxygen

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13
Q

glucose

A

hexose sugar
alpha and beta glucose

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14
Q

uses of water

A
  • as a reactant in cells e.g. photosynthesis, hydrolysis
  • provides structural support in cells
  • keeps organisms cool to maintain an optimum body temperature
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15
Q

properties of water

A
  • metabolic importance
  • high heat capacity
  • heat of vaporisation
  • cohesive properties
  • useful as a solvent
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16
Q

water molecules are made from…

A

2 oxygen
1 hydrogen

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17
Q

what does it mean that water is a polar molecule?

A

oxygen atoms are slightly negatively charged
hydrogen atoms are slightly positively charged

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18
Q

explain hydrogen bonding in water

A

the polarity of water molecules means that a hydrogen atom on one water molecules is attracted to the oxygen atom on another water molecule

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19
Q

hydrolysis reaction

A

a bond is broken and a water molecule is used up
ATP + H20 –> ADP + P + energy

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20
Q

condensation reaction

A

a new bond is formed and a water molecule is released
ADP + P + energy –> ATP + H20

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21
Q

what is the latent heat of vaporisation

A

the amount of energy needed to change 1kg of a liquid to a gas

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22
Q

explain the high heat of vaporisation that water has

A

as liquid water heats up, the hydrogen bonding makes it difficult to separate the water molecules from each other. this means that a lot of energy is needed for water to evaporate
- when water evaporates, energy is used up - this cools the environment where the evaporation is taking place
- this is why sweating helps with body temperature regulation

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23
Q

what is specific heat capacity?

A

the amount of heat 1kg of a substance must absorb or lose to change its temperature by 1oC

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24
Q

explain the high heat capacity of water

A

water has a high heat capacity so takes a long time to heat and cool
- the SHC of water is much larger than sand - land cools faster than the sea
- water is used by warm blooded animals to more evenly disperse heat in their bodies

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25
Q

explain water being a good solvent

A
  • water is a good solvent because ions and polar molecules can easily dissolve in it
  • water is a polar molecule - meaning that the positive end of the water molecule attracts negative ions and the negative ends will attract positive ions
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26
Q

what does cohesion mean?

A

the strong attraction between water molecules due to hydrogen bonds

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27
Q

explain water having cohesive properties

A

cohesion produces surface tension where water meets air
- water forms droplets when placed on a dry surface
- plant use this to help transport water from their roots to their leaves

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28
Q

explain water as a habitat

A
  • water makes an ideal habitat
  • highly stable environment that does not change easily
  • provides a stable habitat for many species
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29
Q

explain formation

A

smaller, biological molecules in an organism’s cells can form larger, molecules that can be used around the body
these biological molecules are important to allow the organism to survive

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30
Q

explain a condensation reaction

A

forms large, biological molecules
releases water
bonds the smaller components together into larger molecules

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31
Q

products of condensation of amino acids

A

produces proteins

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32
Q

products of condensation of two monosaccharides

A

produces disaccharides

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33
Q

products of condensation of fatty acid and monoglyceridess

A

produces lipids

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34
Q

explain breakdown

A
  • when an organism eats, it ingests large, biological molecules
  • these biological molecules are important to allow the organism to survive
  • molecules could be used in the cells for important reaction but are too large to be transported into the cells
  • large molecules must be broken down first
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35
Q

explain a hydrolysis reaction

A
  • breaks down large, biological molecules
  • requires water
  • splits larger molecules into smaller components
  • smaller molecules can easily diffuse into cells or be transported using protein channels
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36
Q

products of hydrolysis of protein

A

produces amino acids

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37
Q

products of hydrolysis of carbohydrate

A

produces disaccharides and monosaccharides

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38
Q

products of hydrolysis of lipids

A

produces fatty acids and monoglycerides

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39
Q

disaccharide definition

A

two monosaccharides joined together

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40
Q

examples of monosaccharides

A

simple sugars
- glucose
- galactose
- fructose

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41
Q

structure of glucose

A

hexose sugar with the chemical formula C6H12O6

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42
Q

function of glucose

A

important source of energy in humans
during cellular respiration, the energy released from glucose helps to make ATP

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43
Q

what are isomers?

A

have the same molecular formula but a different arrangement of atoms in space
e.g. alpha and beta glucose

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44
Q

alpha and beta glucose

A

carbon atoms are numbered from 1-6 and the OH (hydroxyl) groups are in a different orientation around C1

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45
Q

what is a pentose sugar?

A

monosaccharides that have five carbon atoms in their structure e.g. ribose

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46
Q

what is ribose

A

a pentose sugar that is one of the three main components of the nucleotides found in RNA and DNA

47
Q

maltose equation

A

glucose + glucose –> maltose

48
Q

sucrose equation

A

glucose + fructose –> sucrose

49
Q

lactose equation

A

glucose + galactose –> lactose

50
Q

functions of disaccharides

A

sucrose is table sugar
lactose is found in milk

51
Q

what is lactose intolerance?

A

common problem where the body is unable to digest lactose

52
Q

what are polysaccharides?

A

made of two or more monosaccharides joined together by glycosidic bonds
chain may be branched or unbranched
chain may contain different types of monosaccharides

53
Q

examples of polysaccharides

A

starch
glycogen
cellulose
chitin

54
Q

what are glycosidic bonds?

A

monosaccharides form glycosidic bonds with neighbouring monosaccharide molecules to form polysaccharides
-OH groups from neighbouring monosaccharides undergo a condensation reaction to form an O-link between two monosaccharides with water being released

55
Q

how to break a glycosidic bond?

A

reverse reaction of hydrolysis occurs during which water is added

56
Q

what does ATP stand for?

A

adenosine triphosphate

57
Q

what is starch?

A

a polysaccharide formed by condensation reactions of alpha-glucose molecules

58
Q

functions of starch

A
  • main energy storage material in plants
  • stored in seeds of plants
  • broken down into glucose by plants when they need more energy
  • can act as a source of food for humans and animals
59
Q

properties of starch

A
  • does not change the water potential in a cell because its insoluble in water
  • made up of amylopectin and amylose - both alpha-glucose polysaccharides
60
Q

what is amylopectin?

A
  • highly branched chain of alpha-glucose monomers
  • branched structure means that enzymes can easily access the glycosidic bonds and so the glucose molecules can be quickly released when needed
61
Q

what is amylose?

A
  • linear chain of alpha-glucose monomers
  • glucose chains have a helical structure meaning that the amylose strands can pack closely together making this form of starch good for storage
62
Q

test for the presence of starch

A
  1. place a small sample into the dimple of a spotting tile or to a boiling tube
  2. add a few drops of iodine and observe any colour change
    if starch is present, solution will change from orange –> blue-black
63
Q

amylopectin structure and function

A

long, branched structure that makes it ideal for quick energy release

64
Q

amylose structure and function

A

long, unbranched, helical structure that makes it ideal for storage

65
Q

what is glycogen?

A

formed by condensation reactions of alpha-glucose molecules and is the main energy storage material in animals

66
Q

function of glycogen

A
  • highly branched molecule similar to amylopectin
  • when animals need to release energy, glycogen’s highly branched structure means that glucose can be released fast
67
Q

how is glycogen used in the human body?

A
  • good storage molecule as its compact
  • when blood glucose levels decrease, glycogen is broken down to release glucose - glycogenolysis
68
Q

what is cellulose?

A

major component of cell walls in plants

69
Q

structure of cellulose

A
  • long chain of beta-glucose
  • beta-glucose molecules are linked by glycosidic bonds to form linear cellulose chains that are unbranched
  • microfibrils are strong fibers that are made of many cellulose chains that are held together by hydrogen bonds
70
Q

function of cellulose

A
  • most abundant natural polymer
  • the cell walls of plant cells are mostly made of cellulose
  • these cell walls offer structural support because of the strength of the microfibril fibres that they are made of
71
Q

digestion of cellulose

A

cannot be broken down by human digestive enzymes
herbivores like cows and horses are able to digest plant material rich in cellulose

72
Q

what are triglycerides?

A

type of lipid that are mainly used as energy storage molecules

73
Q

how are triglycerides formed?

A

formed by the condensation of one molecule of glycerol and three molecules of fatty acid
ester bonds form between the glycerol and the fatty acid chains
one water molecule is released per ester bond
so three molecules of water are released per triglyceride formed

74
Q

structure of fatty acids

A
  • have long ‘tails’ made of a chain of hydrocarbons with 4-36 carbon atoms
  • the hydrocarbon tail is variable but most fatty acids contain 12-18 carbons
  • glycerol links to the central carbon atom on fatty acids
75
Q

types of fatty acids

A

saturated and unsaturated

76
Q

functions of triglycerides: energy release

A
  • chemical energy is stored in the fatty acid hydrocarbon tails
  • so lost of energy is released when triglycerides are broken down
77
Q

functions of triglycerides: energy

A
  • lipids contain lots of energy
78
Q

function of triglycerides: repel water

A
  • lipid micelle structure
  • insoluble in water because fatty acid tails are hydrophobic
  • means that the cell’s water potential is not affected by triglycerides
  • this is important so that water does not enter the cell through osmosis
79
Q

function of triglycerides: lipid droplets

A
  • in cells, the insoluble triglycerides crowd together as droplets because the hydrophobic fatty acid tails face inwards
80
Q

what are phospholipids?

A

type of lipid that forms a bilayer
main component of cell membranes and are responsible for controlling what goes into and out of cells

81
Q

structure of phospholipids

A
  • composed of fatty acid chains attached to glycerol
  • two hydrophobic fatty acid tails and a hydrophilic phosphate group
  • both hydrophobic and hydrophilic - amphipathic molecule
82
Q

difference between the structure of phospholipids and triglycerides

A

both: composed of fatty acid chains attached to glycerol
difference: one of the three hydrophobic fatty acid tails is replaced by a hydrophilic phosphate group in phospholipids

83
Q

hydrophobic tail of phospholipid

A
  • two fatty acid chains
  • two fatty acid chains are hydrophobic and cannot interact with water
  • in membranes, the hydrophobic fatty acid tails face inside the cell - meaning that water-soluble substances can’t pass through easily
84
Q

hydrophilic head of phospholipid

A
  • the modified phosphate group in phospholipids is hydrophilic and can interact with water
  • in membranes, the hydrophilic phosphate group faces outside
85
Q

what is a saturated fatty acid?

A

when there are only single bonds between carbon atoms in the hydrocarbon chain

86
Q

structure of saturated fatty acids

A
  • carbon atoms are not joined by double bonds in saturated fatty acids
  • the number of hydrogen atoms attached to the carbon skeleton is maximised. this means the fatty acid is saturated
87
Q

function of saturated fatty acids

A
  • saturated fats are solid at room temp and usually of animal origin
  • linked to increased risk of cardiovascular disease in humans
  • foods with high proportion of saturated fat include cream, cheese butter etc
88
Q

what is an unsaturated fat?

A

when the hydrocarbon chain contains at least one double bond

89
Q

structure of unsaturated fats

A
  • have one or more double bonds between carbon atoms in the hydrocarbon chain
  • foods with unsaturated fatty acids include cooking oil
90
Q

why are unsaturated fats liquid at room temp?

A

double bonds kink the carbon chain so unsaturated fats cannot pack together tightly

91
Q

structure of proteins

A
  • made up of amino acids
92
Q

what are dipeptides?

A

formed from the condensation of two amino acids

93
Q

what are polypeptides?

A

formed by the condensation of many amino acids

94
Q

structure of amino acids

A
  • each amino acid has a central carbon atom (alpha carbon)
  • four groups of atoms bonded to the central carbon atom
    an amino group
    a carboxyl group
    a hydrogen atom
    a side group
95
Q

what are the four atoms or groups of atoms bonded to the alpha carbon in an amino acid?

A

NH2 - an amino group
COOH - a carboxyl group
H - a hydrogen atom
R - a side group

96
Q

what is the R group in amino acids?

A

different in each amino acid
determines how the amino acid interacts and bonds with other amino acids in the polypeptide

97
Q

essential amino acids

A

there are 20 different types of amino acids
9 of which are essential in humans because the human body cannot produce them and they are obtained from diet

98
Q

what is glycine?

A

an example of an amino acid
has a hydrogen atom in its R group
the only amino acid that does not have a carbon atom in its R group

99
Q

what are polypeptides?

A

made from chains of amino acids
amino acids are at the end of each polypeptide chain
these amino acids form the two end terminals:
- N-terminal (amine terminal)
- C-terminal (carboxyl terminal)

100
Q

explain how a peptide bond is formed

A

when two amino acids react together, a bond forms between the carboxyl group and the amino group
one water molecule is released as a by-product
the bond formed between two amino acids is a type of covalent bond

101
Q

primary structure of proteins

A

amino acids in a polypeptide chain are arranged in a specific sequence
primary structure is determined by the gene encoding the protein

102
Q

explain the importance of primary structure

A
  • a change in the nucleotide sequence of the gene’s coding region may lead to a different amino acid being added to the growing polypeptide chain
  • a change in the amino acids in a protein could change the protein’s structure and function
103
Q

hydrogen bonding in proteins

A

amino acids in a polypeptide chain can form hydrogen bonds between other amino acids within the chain
hydrogen bonds cause the protein to fold into specific structures

104
Q

secondary structure of proteins

A

folding of the polypeptide determines its secondary structure
many bonds throughout the molecule leads to high stability
may be decreased by environmental factors that weaken the hydrogen bonds e.g. temperature

105
Q

types of secondary structures

A

alpha-helix
beta-pleated sheet

106
Q

tertiary structure of proteins

A

interactions between R groups creates the complex 3D tertiary structure of proteins
usually coiled or folded
many weak and strong interactions that determine the final 3D shape of a protein - when the 3D shape is lost, it may no longer be functional

107
Q

ionic bonds

A

charged amino acids have a positively or negatively charged ion in their side chain which can form relatively strong ionic bonds with other charged amino acids
ionic bonds between amino acids are quite rare

108
Q

disulfide bridges

A

these are covalent bonds set up within proteins containing cysteine amino acids

109
Q

hydrogen bonds in proteins

A

formed between amino acids
relatively weak but when there are many, the overall stability of the tertiary structure increases

110
Q

quaternary structure of proteins

A

multiple 3D polypeptides can come together to form a complex, quaternary structure

111
Q

examples of proteins with a quaternary structure:

A

insulin
collagen
haemoglobin

112
Q

examples of proteins with a quaternary structure: insulin

A
  • weak interactions between the subunits in the insulin polypeptide help to stabilise the quaternary structure
  • insulin has a combination of hydrogen bonds and disulfide bridges that cause it to form a clumped, globular shape
113
Q

examples of proteins with a quaternary structure: collagen

A

fibrous protein found in skin

114
Q

examples of proteins with a quaternary structure: haemoglobin

A

contains four polypeptides surrounding a central haem group