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1 - Biological Molecules Flashcards

1
Q

Monomers

A

Smaller units from which larger molecules are made

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2
Q

Polymers

A

Molecules made from a large number of monomers joined together

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3
Q

Condensation reaction

A

Joins 2 molecules together with the formation of a chemical bond

Elimination of water

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4
Q

Hydrolysis reaction

A

Breaks a chemical bond between two molecules and involves the use of a water molecule

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5
Q

Common Monosaccharides

A

Glucose

Galactose

Fructose

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6
Q

What is formed in a condensation reaction between 2 monosaccharides?

A

Glycosidic bond

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7
Q

Maltose

A

Glucose + Glucose

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8
Q

Sucrose

A

Glucose + fructose

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9
Q

Lactose

A

Glucose + Galactose

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10
Q

How are polysaccharides formed?

A

Condensation of many glucose units

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11
Q

What types of glycogen forms glucose and starch?

A

Alpha Glucose

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12
Q

What type of glucose forms Cellulose?

A

Beta glucose

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13
Q

Formation of triglycerides

A

Condensation of one molecule of glycerol and 3 molecules of fatty acid

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14
Q

What is formed in a condensation reaction between glycerol and a fatty acid?

A

Ester bond

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15
Q

Structure of a fatty acid R group

A

Saturated or unsaturated

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16
Q

Monomer of proteins

A

Amino acids

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17
Q

What is formed in a condensation reaction between 2 amino acids?

A

Peptide bond

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18
Q

What does a functional protein contain?

A

One or more polypeptide

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19
Q

Role of an enzyme

A

Lowers the activation energy of the reaction it catalyses

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20
Q

What are ribosomes formed from?

A

RNA + proteins

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21
Q

Nucleotide structure

A

Pentose sugar

Phosphate group

Nitrogenous base

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22
Q

Structure of a DNA molecule

A

Double helix with 2 polynucleotide chains held together by hydrogen bonds between specific complementary base pairs

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23
Q

What the semi-conservative model of DNA replication ensure?

A

Genetic continuity between generations of cells

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24
Q

Structure of ATP

A

Adenine

Ribose

3x Phosphate groups

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25
What can the hydrolysis of ATP be coupled with?
Energy-requiring reactions within cells
26
Use of inorganic phosphate released during the hydrolysis of ATP
Phosphorylate other compunds, often making them more reactive
27
Enzyme used in ATP hydrolysis
ATP hydrolase
28
Enzyme used in ATP resynthesis
ATP synthase
29
5 Main properties of water
Metabolite Solvent High specific heat capacity High latent heat of vaporisation Cohesive properties
30
Water as a metabolite
Water is a metabolite in many metabolic reactions, including hydrolysis and condensation
31
Water as a solvent
Water is an important solvent where many metabolic reactions occur
32
Water - high specific heat capacity
Buffers changes in temperature
33
Water - large latent heat of vaporisation
Provides a cooling effect with little loss of water through evaporation
34
Water - cohesive properties
Supports columns of water in tube-like transport cells of plants and produces surface tension where water meers air
35
Where do inorganic ions occur?
In the cytoplasm and body fluids of organisms
36
Biochemical test for a reducing sugar
Add Benedicts solution Heat Red = reducing sugar present
37
Biochemical test for non-reducing sugar
Add dilute HCl Neutralise Heat Red = non-redusing sugar present
38
Emulsion test for lipids
Add ethanol + Shake Add water Milky white emulsion
39
What proteins have the tertiary structure as their final structure?
Proteins with only one polypeptide chain
40
What amino acids are repelled from water?
Hydrophobic (non-polar) amino acids SSuch as valine and proline
41
What happens to hydrophobic amino acids?
They get pushed 'inside' the protein due to water molecules in their environment
42
Where do hydrophobic forces occur?
Between non-polar amino acids
43
What do ionic bonds result from?
Electrostatic interactions between electrochemically charged side-chains of amino acids
44
Role of ionic bonds in protein structure
Contribute to the folding process of the tertiary tructure
45
What are disulfide bridges?
Covalent bonds which form between cysteine residues
46
Cysteine
The only amino acid that contains sulfhydryl groups (-SH)
47
What happens when 2 cysteines are in close proximity?
The sulfur atom of one cysteine can covalently bond with a sulfur atom of the neighboring cysteine to produce a disulfide bond
48
Biuret test for proteins
Add NaOH to make solution alkaline Add Copper (II) Sulphate Purple = peptide
49
Quaternary Protein structure
The way in which polypeptide chains come together to form the final protein structure
50
How are different polypeptide chains bonded?
Hydrogen bonds Covalent bonds Ionic bonds
51
homomer proteins
Polypeptide chains are all identical
52
Heteromer proteins
The polypeptide chains are non-identical
53
What type of protein is haemoglobin?
Tetrameric heteromer
54
Enzymes
Globular proteins which play a role as biological catalysts
55
How are metabolic pathways controlled?
enzymes in a biochemical cascade of reactions
56
Intracellular enzymes
Produced and function inside of the cell
57
Extracellular enzymes
Secreted by cells and catalyse reactions outside cells
58
Example of an intracellular enzyme
Catalase
59
Example of an extracellular enzyme
Amylase
60
Role of Catalase
Converts hydrogen peroxide into water and oxygen, preventing any damage to cells or tissues
61
Why is digestion usually carried out by extracellular enzymes?
The macromolecules being digested are too large to enter the cell
62
Role of Amylase
Carbohydrate digestion Hydrolyses starch into simple sugars
63
Production of Amylase
Secreted by salivary glands and the pancreas, for digestion of starch in the mouth and small intestine respectively
64
Catabolic reactions
Involve the breakdown of complex molecules into simpler products Happens when a single substrate is drawn into the active site and broken apart into 2 or more distinct molecules
65
Examples of catabolic reactions
Cellular respiration Hydrolysis
66
Anabolic reactions
Building of more complex molecules from simpler ones Draws 2 or more substrates into the active site, forming bonds between them and releasing a single product
67
Examples of anabolic reactions
Protein synthesis Photosynthesis
68
Induced-fit m odel
States a substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis
69
5 Factors effecting the rate of enzyme-controlled reactions
Enzyme conc Substrate conc Conc of competitive and non-competitive inhibitors pH Temperature
70
Primary protein structure
Amino acid base sequence in the polypeptide chain
71
Secondary protein structure
Folds in the polypeptide chain due to interactions between the amine and carboxyl group alpha-helix beta-pleated sheet
72
Tertiary protein structure
Further folding of the secondary protein structure
73
What stabalises the tertiary protein structure?
H-Bonds Electrostatic forces Disulphide linkages Van Der Waals
74
What shapes does the tertiary protein structure give rise to?
Fibrous Globular
75
Quaternary Protein Structure
3D shape - a protein made up of more than 1 polypeptide
76
Process of DNA Replication
1. Double Helix Unwinding 2. Semi-Conservative Replication 3. DNA polymerase
77
Double Helix Unwinding
H Bonds broken DNA helicase
78
DNA helicase
Unwinds the DNA by breaking the H bonds between complementary base pairs on the 2 polynucleotide chains
79
Why does unwinding of DNA only happen in one region of the molecule at a time?
Ensure stability of the molecule
80
Name of the unwound region of DNA
Replication fork
81
Semi-conservative Replication
Each original strand of DNA acts as a template for the synthesis of the new strands Each new DNA molecule is made up of one parent strand and one daughter strand
82
DNA polymerase
Catalyses condensation reactions, joining complementary nucleotides
83
DNA polymerase vs DNA ligase
DNA polymerase reads DNA ligase catalyses
84
Use of Calcium ions in physiological functions
Helps insulin to be released from the pancreas Responsible for transmitting nerve impulses
85
What enzymes require calcium ions as a cofactor?
Enzymes involved in blood clotting
86
Calcium - bones
Calcium ions are required for bone formation Bones are the major store site for calcium in the body
87
What part of plants does calcium make up?
Middle lamellae
88
Middle lamella
A layer in plant cells that joins 2 plant cells walls together
89
What is the middle lamellae made up of?
Calcium and Magnesium ions
90
Role of Sodium Ions
Co-transport Nervous system (and potassium ions) Fluid regulation
91
Sodium Ions in co-transport
Help molecules such as glucose and amino acids across the cell membrane in order to enter a cell
92
Sodium and potassium in the nervous system
Communication between neurones
93
Sodium in fluid regulation
Movement of water follows the movement of salt When sodium Ions leave the cell, so does water, and the volume of extracellular fluid increases
94
Roles of potassium ions
Nerve impulse and fluid balance Muscle contraction Photosynthesis
95
Potassium ions in nerve impulse and fluid balance
Helps generate nerve impulses Movement is tightly controlled to regulate fluid levels
96
Potassium in photosynthesis
Responsible for opening and closing of the stomata in leaves, controlling CO2 intake
97
Potassium in muscle contraction
Essential for contraction of muscle fibres Potassium levels can affect how well key muscular organs can function
98
Roles of Hydrogen ions
Control pH in digestion Respiration
99
Role of Hydrogen ions in digestion
Maintaining low pH of the gastric juices within the stomach which is important for digestion
100
Role of Hydrogen ions in respiration
ATP synthesis in the mitochondria during cellular respiration
101
Roles of Magnesium Ions
Cofactors Photosynthesis
102
Magnesium ions as cofactors
Cofactors for enzymes such as amylase and lipase which breakdown glucose and fats
103
Magnesium ions in photosynthesis
Production of chloroplasts in plants
104
Role of Ammonium ions in plants
Plants absorb ammonium from the soil, and is able to use the Nitrogen from it to synthesised necessary biological molecules such a as nucleic acids and amino acids

Biology (7 decks)

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