2.1.2: Biological Molecules Flashcards

1
Q

What are the bonds within a H20 molecule ?

A

Covalent

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2
Q

Why does the polarity within a H20 molecule exist ?

A

Cloud of electrons shifted towards oxygen creating regions or negativity and positivity

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3
Q

How does water bond to other water molecules ?

A

Hydrogen bond
(dipoles and lone pairs)

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4
Q

Describe water as a transport medium in eukaryotes

A
  • Blood of animals
  • Xylem of phloem due to cohesion as water molecules are attracted to eachother and hydrogen bond resulting in a continuous column of water called capillary action
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5
Q

Describe water as a habitat in eukaryotes

A
  • High SHC ( many hydrogen bonds which require a lot of energy to break) which is a buffer for temperature for aquatic organisms
  • Cohesion ( attraction between adjacent molecules) creates surface tension so small invertebrates can live on the surface and not be eaten by predators
  • Ice less dense than liquid water due to as they freeze molecules spread out and form hydrogen bonds in lattice structure at fixed distances.Water below still liquid so nutrients can circulate + higher temp so organisms don’t freeze
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6
Q

Describe water as a coolant in eukaryotes

A
  • High SHC ( lots of energy to break many hydrogen bonds) .Ensures internal temperatures of eukaryotes are stable so enzymes don’t denature
  • High latent heat of vapourisation ( lots of energy to convert liquid water to it’s gaseous state due to energy to break hydrogen bonds between molecules ).Cooling mechanism in eukaryotes as water in sweat absorbs heat as it evaporates
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7
Q

Describe advantages of water’s properties to prokaryotes

A
  • Solvent to transport nutrients across the cell surface membrane for metabolic reactions (aerobic respiration)
  • Stable internal temperature for enzyme activity
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8
Q

Describe water’s solubility in terms of eukaryotes

A
  • For ionic/ polar substances that can bond with water
  • Transporting phosphates through the xylem to make phospholipids
  • Transporting glucose through the blood stream for respiration
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9
Q

Which elements are in carbohydrates ?

A

C,H,O

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10
Q

Which elements are in lipids ?

A

C,H,O

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11
Q

Which elements are in proteins

A

C,H,O,N,S

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12
Q

Which elements are in nucleic acids ?

A

C,H,O,N,P

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13
Q

Give 2 properties of glucose

A
  • SOLUBLE so can be dissolved and absorbed into bloodstream of animals for respiration
  • SMALL to diffuse easily across membranes
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14
Q

Give the 3 monosaccharides

A
  • Glucose
  • Fructose
  • Galactose
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15
Q

Give the 3 disaccharides

A
  • Maltose
  • Sucrose
  • Lactose
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16
Q

Give the 3 polysaccharides

A
  • Glycogen
  • Cellulose
  • Starch
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17
Q

How is a glycosidic bond formed and broken ?

A

Condensation reaction
Hydrolysis reaction

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18
Q

Define condensation reaction

A

Joining 2 molecules together by removing H20 - chemical bond is formed

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19
Q

Define hydrolysis

A

Splitting apart molecules through addition of H20 - chemical bond is broken

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20
Q

Glucose + glucose =

A

maltose + H20

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21
Q

Glucose + galactose =

A

lactose + H20

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22
Q

Glucose + fructose =

A

sucrose + H20

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23
Q

Define and give an example of a hexose monosaccharide

A
  • 6 carbon atoms in ring
  • Glucose
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24
Q

Define and give an example of a pentose monosaccharide

A
  • 5 carbon atoms in ring
  • Ribose
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25
Q

What are the 3 polymers of glucose ?

A
  • Starch
  • Cellulose
  • Glycogen
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26
Q

What is the polymer of an amino acid ?

A

Protein

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27
Q

What are the 2 polymers of nucleotides ?

A
  • DNA
  • RNA
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28
Q

What are the 2 isomers of C6H1206 ?

A
  • Alpha glucose
  • Beta glucose
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29
Q

What is the difference between alpha and beta glucose ?

A

Alpha glucose has the OH on C1 below the plane of the ring whereas beta glucose has the OH on C1 above the plane of the ring

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30
Q

Define metabolism

A

Sum total of all chemical reactions that take place within a cell

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31
Q

Define catabolic reaction

A

Metabolic reactions involved in breaking down larger molecules into smaller ones

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32
Q

Give an example of a catabolic reaction

A

Digestion

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33
Q

Define anabolic reaction

A

Building of larger molecules from smaller ones

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34
Q

Give an example of an anabolic reaction

A

Amino acids into proteins in ribosomes

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35
Q

Define monomer

A

Smaller units which can create larger molecules

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36
Q

Define polymer

A

Made from lots of monomers bonded together

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37
Q

What monomer is starch made of ?

A

Alpha glucose

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38
Q

Describe the structure of amylose

A

Unbranched helix with 1,4 glycosidic bonds

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39
Q

Describe the structure of amylopectin

A

Branched molecule with 1,4 and 1,6 glycosidic bonds

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40
Q

What is the function of starch ?

A

Store of glucose in plants

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41
Q

How does the structure of starch relate to it’s function ?

A
  • HELIX = compact to fit lots in a small space
  • BRANCHED = increases SA for rapid hydrolysis back to glucose
  • INSOLUBLE = wont affect water potential
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42
Q

What monomer is glycogen made from ?

A

Beta glucose

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43
Q

Describe the structure of glycogen

A

1,4 and 1,6 glycosidic bonds

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44
Q

What is the function of glycogen ?

A

Store of glucose in animals found in muscle and liver cells

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45
Q

How does the structure of glycogen relate to it’s function ?

A
  • HIGHLY BRANCHED = increases SA for rapid hydrolysis back to glucose
  • INSOLUBLE = won’t affect water potential
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46
Q

What are advantages of glycogen’s structure compared to amylopectin ?

A

More branched so higher rate of respiration for more muscle contraction, movement and mobility in animals

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47
Q

What monomer is cellulose made from ?

A

Beta glucose

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48
Q

What is the structure of cellulose ?

A
  • 1,4, glycosidic bonds
  • Polymer forms long straight chains which are held in parallel by hydrogen bonds to form fibrils. Macrofibrils combine to form cellulose fibers
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49
Q

What is the function of cellulose ?

A

Structural strength for plant cell walls

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50
Q

How does the structure of cellulose relate to it’s function ?

A
  • MANY HYDROGEN BONDS = collective strength to withstand turgor pressure
  • INSOLUBLE = wont affect water potential
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51
Q

Describe features of lipids

A
  • Macromolecules
  • Insoluble in water
  • Hydrophobic
  • Fatty acids + glycerol
  • Dissolve in organic solvents e.g. ethanol
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52
Q

What is glycerol composed of ?

A

Alcohol with 3 carbons ( each with an OH group) and single covalent bonds

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53
Q

Describe the polarity of a phospholipid

A

Polar

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54
Q

Describe the polarity of lipids

A

Non-polar

55
Q

Describe the features of a phospholipid

A
  • Modified triglyceride
  • Phosphate group replaces 1 fatty acid chain
  • Fatty acid chains (2) = non-polar / hydrophobic
  • Phosphate group (1) = polar / hydrophilic
56
Q

Describe features of sterols

A
  • 4 carbon rings and a hydroxyl group
  • Hydrophobic and hydrophilic regions ( OH group)
57
Q

Define a saturated fatty acid

A

No double bonds between carbon atoms

58
Q

Define mono/poly unsaturated fatty acid

A

One/more than one double bond between carbon atoms

59
Q

What is a disadvantage of unsaturated fatty acids ?

A

Cannot pack together easily

60
Q

What is a triglyceride made of ?

A
  • Glycerol (3)
  • Carboxyl group (3)
  • Hydrocarbon chain (3 fatty acid chains)
61
Q

How is a triglyceride formed ?

A

OH group on carboxyl group reacts with H on glycerol in a condensation reaction forming an ester bond

62
Q

How does the structure of a triglyceride relate to it’s function ?

A
  • TRANSFER ENERGY = large ration of C-H bonds compared to carbon atoms
  • METABOLIC WATER SOURCE = many H-O atoms. Water can be released if oxidised (useful for camels in deserts)
  • INSOLUBLE = as large hydrophobic molecules so won;t affect water potential or osmosis
  • LOW IN MASS = many can be stored without limiting movement in an active mammal
63
Q

Describe the functions of lipids in organisms

A
  • Form membranes and hydrophobic barriers
  • Electrical insulation for impulse transmission
  • Buoyancy for aquatic animals
  • Cushion vital organs
  • Hormone production and regulation
64
Q

How do the structure of phospholipids relate to their function ?

A

Polar so can form a phospholipid bilayer, becoming surfactants which enables compartmentalisation in cells

65
Q

Where is cholesterol made ?

A

Liver and intestines

66
Q

What is the function of cholesterol ?

A

In cell membranes to provide STABILITY and impact FLUIDITY .Reduces membrane fluidity at high temperatures and decreases at lower temperatures to control movement across the membrane

67
Q

What is an amino acid made from ?

A
  • Amine group (NH2)
  • Carboxyl group ( COOH)
  • R group (varies with each amino acid)
68
Q

How many naturally occurring amino acids are there ?

A

20

69
Q

Which amino acid has an R group of H

A

Glycine

70
Q

How many amino acids have sulfur in their R group ?

A

2

71
Q

What is the polarity of an R group containing oxygen ?

A

Polar

72
Q

What is the polarity of an R group not containing oxygen ?

A

Non-polar

73
Q

What does the carboxylic group in an amino acid do ?

A

Acts as an acid ( donated H+ ions)

74
Q

What does the amine group in an amino acid do ?

A

Acts as a base ( receives H+ ions)

75
Q

How are 2 amino acids bonded together ?

A

OH on carboxyl group reacts with H on amine group on another amino acid in a condensation reaction to form a peptide bond

76
Q

What is the test for the presence of peptide bonds ?

A

Reacts with biuret reagent and turns lilac

77
Q

Describe the primary structure of a protein

A

Sequence of amino acids in a polypeptide chain

78
Q

Describe the secondary structure in a protein

A

Sequence of amino acids causes part of protein molecule to bend into an alpha helix or fold into a beta pleated sheet

79
Q

Describe the tertiary structure of a protein

A

Further folding of polypeptide chain held together by bonds forming between R groups. 3D shape is formed

80
Q

Give examples of the tertiary structure of a protein

A

-DISULFIDE BONDS = strong covalent bonds formed between R groups of 2 sulfur containing amino acids
- HYDROPHOBIC AND HYDROPHILIC INTERACTIONS = weak interactions between polar + non polar R groups
Hydrophobic -> point inwards
Hydrophobic -> point outwards
-HYDROGEN BONDS = weak
-IONIC BONDS = stronger bonds formed between two oppositely charged R groups

81
Q

How is the secondary structure of a protein held in place ?

A

Hydrogen bonds

82
Q

Describe the quarternary structure of a protein

A

A protein made of more than one polypeptide chain bonded by R groups

83
Q

How does a globular protein form ?

A

Polypeptide chain rolls up into a spherical shape

84
Q

Give three features of a globular protein

A
  • Water soluble ( hydrophilic R groups are on the outside of protein)
    -Compact
    -Metabolic functions
85
Q

What is the hormonal example of a globular protein ?

A

Insulin

86
Q

What is the function of insulin ?

A

Hormone for regulating blood glucose concentration

87
Q

Give 2 ways the structure of insulin benefits its function

A
  • Soluble so can be transported in the bloodstream
  • Precise shape to bind to specific receptors on cell surface membrane
88
Q

What is the enzyme example of a globular protein ?

A

Catalase

89
Q

What is the function of catalase ?

A

Enzyme to catalyse reactions

90
Q

Outline the structure of catalase

A

Quaternary structure - 4 prosthetic haem groups/polypeptides with Fe2+ ions

91
Q

How does the structure of catalase benefit it’s function ?

A
  • Soluble so can be transported in the bloodstream
  • Fe2+ ions allow enzyme to interact with hydrogen peroxide and speed up it’s breakdown as it is toxic /damaging to cells
92
Q

Give the equation for the breakdown of hydrogen peroxide by catalase

A

2H2O2 —> O2 +2H2O

93
Q

What is a conjugated protein ?

A

Globular proteins that contain a non-protein component

94
Q

What is an example of a conjugated protein ?

A

Haemoglobin

95
Q

What is the function of haemoglobin

A

Oxygen carrying pigment in red blood cells

96
Q

Outline the structure of haemoglobin

A

-Quaternary protein
-4 polypeptides
-2 alpha polypeptides + beta polypeptides
-Each sub unit contains a prosthetic haem group which has Fe2+ ions present

97
Q

What is the function of Fe2+ ions inn the haem groups within haemoglobin ?
Give an equation

A

Combine reversibly with oxygen so haemoglobin can be transported to cells
( Hb + 4O2 REVERSIBLE HbO8 )

98
Q

Describe the formation of a fibrous protein

A

Polypeptide chains form long twisted strands that are linked together

99
Q

Describe the structure / features of a fibrous protein

A
  • Stable and strong structure
  • Insoluble in water
  • Limited range of amino acids with small R groups ( hydrophobic)
  • Often don’t have tertiary structure
100
Q

What are the examples of fibrous proteins ?

A

Elastin, collagen and keratin

101
Q

Where is elastin found ?

A
  • Elastic fibres
  • Walls of blood vessels
  • Alveoli
102
Q

What are the features/function of elastin ?

A
  • Provide structural strength
  • Can expand and recoil
103
Q

Describe the structure of elastin

A

Quarternary protein made from tropoelastin

104
Q

Where is collagen found ?

A
  • Connective tissue
  • Skin
  • Tendons , ligaments
  • Nervous system
105
Q

Describe the structure/features of collagen

A

3 polypeptides wound together as long, strong flexible rope

106
Q

Where is keratin found ?

A
  • Hair
  • Skin
  • Nails
107
Q

Describe the structure of keratin

A
  • Group of fibrous proteins
  • Many sulfur containing amino acids
  • Many disulfide bonds whose bond angle determines flexibility
108
Q

Give 3 features of keratin

A
  • Strong
  • Inflexible
  • Insoluble
109
Q

Give the formula and 2 functions of calcium ions

A

Ca2+
- Synapsis transmission
- Muscle contractions

110
Q

Give the formula and 2 functions of potassium ions

A

K+
- Stomatal opening
- Nerve impulse transmission

111
Q

Give the formula and 2 functions of chloride ions

A

Cl-
- Inhibitory effect at a synapse
- Provides negative charge to balance sodium and potassium ions in cells

112
Q

Give the formula and function of nitrate ions

A

NO3-
- Absorbed by plants through root hair cells to make amino acids

113
Q

Give the formula and 3 functions of a sodium ion

A

Na+
- Co-transport of glucose and amino acids
- Nerve impulse transmission

114
Q

Give the formula and 3 functions of hydrogen ions

A

H+
- Involved in chromosomes
- Determines pH
- Catalyses reactions

115
Q

Give the formula and 3 functions of ammonium ions

A

NH4+
- Nitrogen cycle ( bacteria convert ions into nitrate ions)
- Result of decay of amino acids in decomposition and deamination

116
Q

Give the formula and 2 functions of phosphate ions

A

PO43-
- Involved in formation of phospholipids for cell membranes
- Formation of nucleic acids and ATP

117
Q

Give the formula and 2 functions of hydrogencarbonate ions

A

HCO3-
- Maintains pH of blood
- Provides source of CO2 to plants when dissolved in solution

118
Q

Give the formula and 2 functions of hydroxide ions

A
  • Impacts pH
  • Bonding between biochemical molecules
119
Q

Give the test for the polysaccharide starch

A
  • Add iodine
    Red/brown –> blue/black
120
Q

Give the test for proteins

A
  • Add biuret reagent
    Blue –> lilac
121
Q

Give the test for reducing sugars

A
  • Add Benedicts reagent
  • Heat
    Blue –> Brick red ( range of colours for concentrations)
122
Q

Give 2 examples of reducing sugars

A

Maltose and lactose ( monosaccharides)

123
Q

Give another method of testing for reducing sugars other than benedicts reagent

A

Reagent strip

124
Q

At a molecular level how does benedicts reagent prove the presence of reducing sugars ?

A

Copper ions are reduced from Cu2+ to Cu+

125
Q

Give the test for lipids

A
  • Dissolve sample in ethanol
  • Add distilled water
  • White emulsion forms
126
Q

Give the test for non-reducing sugars after benedicts reagent remains blue

A
  • Add acid
  • Boil
  • Cool solution and add alkali to neutralise
  • Add benedicts
  • Blue –> brick red
127
Q

How does sucrose turn benedicts reagent brick red through the test for non-reducing sugars

A

Sucrose is hydrolysed by an acid (HCl) into glucose and fructose

128
Q

Outline how biosensors work

A
  • Single DNA strand or protein which is complementary to test sample is immobilised
  • Sample binds
  • Binding causes a change in a transducer ,releasing an electric current which determines concentration
129
Q

Summarise the process of biosensors in 2 steps

A
  • Molecular recognition
  • Transduction
130
Q

Give the equation for the Rf in chromatography

A

Distance moved by solvent

131
Q

How are the results from the transduction step in biosensors read ?

A

Colour on test trip or reading on a test machine

132
Q

Give the steps of colorimetery

A

1) Set filter (opposite colour on colour wheel to test sample)
2) Callibrate ma\chine using distilled water
3) Plot a calibration curve using samples of known concentration
4) Measure % transmission of sample after filtering to remove precipitates

133
Q

What does a more concentrated sample mean for a colorimetery reading ?

A

More absorbance and less % transmission