Teaching block 1 Flashcards

part 1 (143 cards)

1
Q

characteristics of life

What are the characteristics of life?

Are viruses alive?

A

M – MOVEMENT
R – RESPIRATION
S – SENSITIVITY

G - GROWTH
R - REPRODUCTION
E – EXCRETION (removing metabolic waste material)
N – NUTRITION

Viruses – may or may not be alive as cannot reproduce without another cell

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2
Q

Cell theory
– Schleiden and Schwann 1839

A
  • All living organisms are composed of one or more cells
  • The cell is the basic unit of structure + organisation in organisms
  • Cells arise from pre-existing cells
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3
Q

Classification?
why its useful?
Who ?

A

Classification - the process of naming + organising organisms into groups based on their characteristics

  • provides a catalogue of past + present species
  • An internationally recognised way of referring to particular organisms = allows scientists around the world to work together

Carl Linnaeus [1707 – 1778]

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4
Q

The binomial system

A
  • Every organism given 2 names : genus name + species name [ Homo sapiens]
  • Binomial names can tell you about the biology of an organism

*

  • must use italics / underline if handwritten
  • genus - starts with CAPTAL LETTER
  • species - starts with lower case
  • after first use, its abbreviated/shortened to initial of genus and then the species name
    [H. sapiens]
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5
Q

The 3 domains?

A
  1. Bacteria
  2. Archaea
  3. Eukaryota
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6
Q

Kingdoms in Eukaryota

A
  1. Animalia
  2. Plantae
  3. Protoctista – Protists – Protozoans
  4. Fungi
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7
Q

Examples of… in pharmacy context

  • Animalia
  • Plantae
  • Protoctista
  • Fungi
  • Prokaryotes
  • Viruses
A
  • Animalia [tapeworms, tics]
  • Plantae [aspirin (Willow Bark), aloe vera, CBD]
  • Protoctista [Malaria protist]
  • Fungi [Athletes foot, ringworm, penicillin]
  • Prokaryotes [Tuberculosis bacteria, ecoli, Salmonella]
  • Viruses [HIV, influenza]
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8
Q

What are the levels of classification?

A

Domain (Dead)

Kingdom (King) KEEPING

Phylum (Phillip) PRECIOUS

Class (Came) CREATURES

Order (Over) ORGANISED

Family (For) FOR

Genus (Goat) GRUMPY

Species (Stew) SCIENTISTS

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9
Q

Classification of human
(Homo sapiens)

A
  • Kingdom - Animalia - capable to move on own
  • Phylum - Chordates - animals with nerve cord / backbone
  • Class - Mammalia - Hair, milk glands
  • Order - Primate - Grasping hands/feet
  • Family - Hominids - “man” (have 3d vision + relatively flat face)
  • Genus - Homo - primitive + modern man (upright posture + large brains)
  • Species - Sapiens - Modern man only (high forehead + thin skull bones)
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10
Q

Species?

A

Species = group of organisms that can interbreed to produce fertile offspring

  • Horse + donkey (separate species) can interbreed to produce a mule which is sterile (infertile)
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11
Q

microscopes

Types of

  1. Light microscope
  2. Electron microscope
A
  1. Light microscope
  • Compound microscope (40x -1000x magnification)
  • Binocular/stereo dissecting microscope (10x – 90x magnification )
  1. Electron Microscope
    [large, expensive + not portable]
  • Transmission electron microscope (TEM)
    = 2 dimensional image + black and white
  • Scanning electrons microscope (SEM)
    = 3 dimensional image + sometimes at a lower
    magnification than TEM
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12
Q
  1. What is the name given to a microscope with one eyepiece?
  2. What is the name given to a microscope with two eyepiece lenses?
A
  1. monocular
  2. binocular, stereo
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13
Q

Light (L) v Electron (E) microscope

  1. Illumination
  2. Focused by
  3. Max magnification
  4. resolving power
  5. specimens living/dead
  6. specimen preparation
  7. Images in colour
A
  1. L = light E = Electrons
  2. L = glass lenses E =electromagnets
  3. L = x1500 E= x50 million
  4. L = 200nm (0.2um) E = 78 picometres (78 x10^-12m)
  5. L = living E = Dead
  6. L = relatively cheap E = expensive
  7. L = yes colour E = No colour (colour added by computer)
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14
Q

Magnification

A

Magnification = Image size / actual size

  • Size of image = Actual size of object × magnification
  • scale bar shows actual size = measure in mm = convert to um

Total magnification = Objective lens x Eyepiece lens

  • Magnification of the object lens is written as Mo
    Eg Mo= x40
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15
Q

Units Conversions

A

Km [x1000] > m [x10] >dm [x10]> cm [x10]> mm [x1000]> um [x1000]> nm

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16
Q

labelled plant cell under microscope

A
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17
Q

cell structures within electron microscope

Function of Nucleus + what it’s made of

[be able to draw a labelled nucleus]

A

Nucleus controls the activities of the cell, contains the genetic information (DNA)

Made up of …

  • Chromatin [2 types]
    1. Heterochromatin
    2. Euchromatin
  • Nucleolus
  • Nuclear pores
  • Nuclear membrane
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18
Q

What are…

  • Chromatin
  • Heterochromatin
  • Euchromatin
  • Nucleolus
  • Nuclear pores
  • Nuclear membrane
A
  • Chromatin – coloured material = DNA spread through nucleus (forms the chromosomes)
  • Heterochromatin – dark staining material, often on edge of nucleus = tightly packed DNA = less active DNA or DNA not being read = silenced genes
  • Euchromatin – lighter coloured DNA = more loosely packed DNA that is being actively read to produce proteins = gene expression
  • Nucleolus – produces ribosomes
  • Nuclear pores = holes through the nuclear membrane – allow ribosomes + mRNA to go from
    nucleus to cytoplasm
  • Nuclear membrane = double membrane around a nucleus. Rough endoplasmic reticulum (RER) joins up to the nuclear membrane
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19
Q

Eukaryotic v Prokaryotic cells

A

Prokaryotic

  • do not have a nucleus but a nucleoid
  • single cells organism, size 1 – 5 μm
  • e.g. bacteria

Eukaryotic
- have a nucleus
- single or multicellular, size 10 - 100 μm
- e.g. plants, animals, fungi, algae

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20
Q

Rough Endoplasmic Reticulum
(Rough ER)

A
  • flattened parallel membranes covered with ribosomes (attached to the rough ER
    membranes)
  • Ribosomes make protein = so the function of rough ER is to make proteins
  • Rough ER is found in eukaryotes so the ribosomes are 80s
  • rough ER can be connected to the nucleur membrane
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21
Q

Smooth endoplasmic reticulum
(smooth ER)

A
  • tubes rather than flattened
  • no ribosomes
  • Function of smooth ER is synthesis + transport of lipids and steroids
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22
Q

Golgi body

A

Discovered by + named after, Camillo Golgi

  • Looks like a stack of saucers
  • A function of the Golgi body is to attach carbohydrates to proteins to make glycoproteins (e.g. mucus)
  • modifies the proteins passing through
  • Has vesicles on edge – carry substances to + from the Golgi body
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23
Q

Synthesis of mucus
+ uses of mucus?

A

Mucus = glycoprotein - used for protection + lubrication + digestive system

  • mRNA goes from nucleus to ribosome (on Rough ER)
  • Protein synthesis occurs In ribosome
  • Vesicle carrying protein pinches off rough ER
  • Protein is carried to the Golgi body
  • Protein joined together to carbohydrates in Golgi body –> making mucus
  • Vesicles containing mucus becomes part of the membrane
  • Mucus is released through cell membrane through exocytosis
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24
Q

ADP + ATP

A

ADP + P –> ATP
–> respiration
<– Energy used in eg muscle contraction

ADP – Adenosine Diphosphate

ATP – Adenosine triphosphate

P – Phosphate

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25
Aerobic respiration in animals + plants
Glucose + oxygen --> water + carbon dioxide (+2880 kJ) C6H12O6 + 6O2 --> 6H20 + 6CO2
26
Anaerobic respiration in animals
Glucose --> lactic acid (+150kJ) C6H12O6 --> 2CH3CH (OH) COO4
27
Anaerobic respiration in plants / yeast
Glucose --> ethanol + carbon dioxide (+210 kJ) C6H12O6 --> 2CH3CH2OH + 2CO2
28
Purpose of respiration?
- to convert energy in glucose into energy in the ATP molecule - = providing energy for cells to function properly by driving cell’s biological processes.
29
Mitochondria structure + function
**Structure**: - Rod-shaped organelles - Matrix – fluid - Cristae – folding of inner membrane - Outer membrane - Granules on cristae = ATP synthase **Function**: - Generation of chemical energy needed to power cell’s biochemical reaction = stored in adenosine triphosphate (ATP) molecule - The biochemical processes are known as cellular respiration - Through: Glycolysis --> Krebs cycle --> Electron transport chain (ETC) in oxidative phosphorylation
30
Lysosome
- Is a vesicle (small membrane enclosed space) that contains digestive enzymes. ‘suicide bags’ Functions: - Digestion of cellular waste + old organelles - Programmed cell death - destroy whole cells in programmed cell death (apoptosis) - Phagocytosis - digest bacteria phagocytosed by white blood cells (leucocytes)
31
Endocytosis = material going into cell 1. Phagocytosis? 2. Pinocytosis?
1. Phagocytosis - cell feeding - uptake of small molecules and extracellular fluids by a cell through the formation of small vesicles 2. Pinocytosis - cell drinking - uptake of large particles, such as cell debris and microorganisms, by a cell through the formation of large vesicles
32
Process of phagocytosis
White blood cells engulfs bacterium = bacterium stored in vacuole --> lysosomes release digestive enzymes to digest bacterium - a white blood cell can digest about 12 bacteria then it dies --> lots of white blood cells = puss
33
Endosymbiosis?
Endo – inside Symbiosis (mutualism) – where 2 organisms live closely together + both benefit - Phagocytosis explains some of the theory of endosymbiosis – if an aerobic respiring bacterium is engulfed it could over evolutionary time become a mitochondrion + if a cyanobacterium was engulfed it could become a chloroplast - Chloroplasts + mitochondria are believed to have been free living bacteria which were phagocytosed / engulfed into a larger cell, but did not get digested. This became a mutualistic or symbiotic relationship - Theory of endosymbiosis first describes by Lynn Margolis
34
Evidence for endosymbiosis
* Chloroplasts + mitochondria are about the same size as prokaryotes * Chloroplasts + mitochondria have a double membrane – so outer membrane believed to have been the vacuole + the inner membrane was the membrane of the bacterium * Ribosomes in chloroplasts and mitochondria are 70 S and in bacteria also 70 S, but 80 S in eukaryotes * Similar DNA - genetic sequencing has shown * Mitochondria + chloroplasts reproduce by binary fission which is how bacteria reproduce
35
Microvilli
- Are difficult to see with a light microscope so are sometimes called a ‘brush border’ - microscopic, finger-like projections on the surface of cells that increase the surface area for absorption or secretion - eg for absorption of digested food in the small intestines 1mm2 of intestines lining has 200 000 000 microvilli
36
Cilia?
- tiny hair-like structures that extend from the surface of cells - used in movement
37
Where are cilia found + why are they useful?
- cells lining the human respiratory system have cilia (cilliated epithelial cells) - they are all covered in mucus which helps trap bacteria + pathogen = cilia move this material along the trachea to the pharynx (throat), where it can be swallowed or coughed up - Paramecium (type of single celled Protozoan) - fresh water unicellular organisms which are covered in cilia for swimming
38
Flagellum? organism which has them?
- hair-like structure - which helps cells move - Euglena – a freshwater organism, has 2 flagellums, used in swimming
39
do drawings for cilia + flagellum structure
40
What's the internal structure of cilia + flagella? How can u tell if the cell has cilia or flagellum?
- Both cilia + flagella have a 9+2 arrangment of microtubules - Microtubules made of protein called tubulin - 9 microtubules around the edge + 2 in the centre - cells normally have one or two flagella or LOTS of cilia = can tell if its cilia if there are lots / its flagella if there are only a few
41
Centrioles Function?
- cyclindrical organelles made of protein tubulin - 2 centrioles per cell - Used in cell division in spindle formation (mitosis + meiosis) - Also involved in the formation of cilia + flagella
42
Centrioles structure
- cyclindrical organelles made of protein tubulin - 2 centrioles per cell - similiar structure to cilia + flagella but without the central microtubules + are arranged in groups of 3 microtubules around the edge of structure - Centrosome = structure made of a pair of a pair of centrioles surrounded by a mass of material
43
Know Plant cell structure - cell wall
- made of cellulose (fibre in human diet) - prevents plant cell from bursting
44
Middle lamella? Plasmodesmata?
- Middle lamella = layer of 'glue' mad of calcium + magnesium pectates, that hold adjacent cells together - Plasmodesmata = a hole through the cell walls. cytoplasm, cell membrane + some organelles (eg smooth ER) can go through these holes
45
Photosynthesis | **photo** - light **synthesis** - making something
- converting light energy into energy in a glucose molecule - occurs in the chloroplast - Carbon dioxide + water (+sunlight to chlorophyll) --> glucose + oxygen - 6CO2 + 6H2O --> C6H12O6 + 6O2
46
Cell fractionation
Extracting / isolating a sample of a particular organelle, so you can research the biochemistry of the organelle
47
Steps for cell fractionisation:
1. Put tissue into ice cold, isotonic buffer 2. Cut tissue into small pieces 3. Put tissue into blender/homogeniser to break up cells 4. Filter to remove debris (waste) 5. Centrifuge – organelles separate out in a particular order due to their density + shape 6. When taking test tube out of centrifuge have a solid pellet (containing specific organelle) at the bottom + a liquid supernatant above 7. Take out supernatant and centrifuge again to get other organelles [Supernatant = a liquid – it may contain organelle that need to be re-spun in a centrifuge]
48
Why do we put tissue into ice cold, isotonic buffer?
- **Low temperature**- slows chemical reactions, preventing self-digestion by enzymes - **Isotonic** - means same water potential = prevents osmosis so organelles do not gain or lose water causing them to shrivel up or burst - **Buffer** - prevents pH change
49
Order of orgnanelles which are first --> last to get seperated Centrifuge setting (g)? [Time (min)?]
1. Nuclei - 800 – 1000g [5-10min] 2. Mitochondria - 10000 - 20000g [15 - 20 min] 3. Lysosomes 4. Rough ER - 50000 – 80000g [30-50 min] 5. Plasma membrane - 80000 – 100000 [60 min] 6. Smooth ER 7. Free ribosomes - 150000 – 300000 [>60]
50
Prokaryotes
- smallest cells are 0-1nm -10μm - So small they don't need a transport system as they can use diffusion - There are lots of them: 1g of soil contains 100 million bacteria 10cm3 of milk (fresh) have 3000 million bacteria - Important in regulating through decay -They can fix nitrogen by converting atmospheric nitrogen into a form plants can use (nitrogen-fixing bacteria)
51
Structures found in a prokaryote
- capsule - peptidoglycan cell wall - Flagella - Pilus (pili) - Plasmid - nucleoid [chromosomes] - Fibriae - Mesosome - Cell membrane - 70s ribosomes
52
Functions of 1. Capsules 2. Cell wall 3. Mesosome
1. **Capsules** protection for cell, including protection from phagocytosis + prevents drying out [capsulated pneumococcal grow in humans causing pneumonia whereas non-capsulate strains are easily destroyed by phagocytic] 2. **Cell wall** made of peptidoglycan or murein (2 diff words for same thing)= cell wall prevents bursting 3. **Mesosome** – for respiration – artifact of electron microscope preparation [cell division, increase SA for aerobic respiration, DNA replication]
53
4. Flagella 5. Pili / pilus 6. fimbria
4. **Flagella** – cell movement - made of proteins called flagellin – no 9+2 arrangement no microtubule. Instead, it rotates. only place in nature where you get a wheel 5. **Pili** (singular pilus) or **fimbria** make cells sticky + are involved in cell to cell surface contact. - F-pilus is allows DNA to move from 1 bacterial cell to another in sexual reproduction
54
Characteristics in Prokaryotes V Eukaryotes 1. Size 2. Form 3. Ribosome size 4. Endoplasmic reticulum 5. Organelles
1. **Size** Prokaryotes - 0.5 - 5 um Eukaryotes - up to 40 um 2. **Form** Prokaryotes - Unicellular / filamentous Eukaryotes - Unicellulat/ filamentous/ multicellular 3. **Ribosome size** Prokaryotes - 70S Eukaryotes - 80S 4. **Endoplasmic reticulum** Prokaryotes - Not present Eukaryotes -Present 5. **Organelles** Prokaryotes - Few, no double membrane Eukaryotes -Many + some with double membrane
55
6. Cell walls 7. Flagella 8. Respiration 9. Photosynthesis 10. Nitrogen Fixing
6. **Cell walls** Prokaryotes - Yes: peptidoglycan / murein Eukaryotes - Plant cell: cellulose 7. **Flagella** Prokaryotes - Yes but no microtubules + have flagellin Eukaryotes - Yes but 9+2 arrangment of microtubules 8. **Respiration** Prokaryotes - Uses mesosomes Eukaryotes - Use mitochondria 9. **Photosynthesis** Prokaryotes - Uses photosynthetic membranes not chloroplast Eukaryotes - Use chloroplast 10. **Nitrogen Fixing** Prokaryotes - Some bacteria can fix nitrogen Eukaryotes - No eukaryotes can fix nitrogen
56
Viruses origin
- First discovered in 1890s by Russain scientist Ivanovski - He discovered a disease causing 'thing/agent/microbe' that could pass through a filter that was capable of stopping/trapping bacteria - Viruses are very small- about 10-300 nm - one virus = a virion
57
Bacteriophage
Bacterio - bacterium Phage - other word for virus - Bacteriophage is a virus that can infect a bacterium - They are useful in industrial genetic engineering as they can be used to inject DNA into a bacterium
58
How Bacteriophage injects DNA into a bacterium
1. Phage attaches to the cell wall of bacterium (host) 2. Digestion of bacterial host cell wall 3. Analogous (similar in function but different in structure) to a very thin hypodermic syringe - Bacteriophage's tail contracts + tail core passes through digested cell wall + DNA is injected into host bacterium
59
Lytic cycle
1. Bacteriophage attaches + Adsorption occurs, triggering the release of DNA into bacterium 2. phage (virus) DNA replicates 3. New virus heads appear 4. New completed phages (viruses) assembled 5. Lysis – bacterial cell bursts = releasing viruses which infect more bacteria
60
Nitrogen fixing bacteria
- Some prokaryotes can fix nitrogen + live in the root nodules of legumes (peas + beans) - legumes are eukaryote = example of a symbiotic / mutualistic relationship = the plant + the bacteria benefit [ plants get nitrogen + bacteria get sugars/place to live from plant + humans get nitrogen from plants essential for amino acids/proteins as there is nitrogen in all amino acid molecules ] - Nitrogen fixing bacteria are very important for human nutrition as we need nitrogen to make protein - bacteria are often very beneficial organisms + not something to be seen as bad and therefore need to be killed
61
# exam question Q. Some food crop plants have bacteria living in root nodules. What do these bacteria do? How do the bacteria, the plant and people benefit from thisprocess? (5 marks)
- Bacteria fix nitrogen (1 mark) - symbiosis/mutualism (1 mark) - plants get nitrogen (1 mark) - bacteria get sugars/place to live from plant (1 mark) - humans get nitrogen from plants essential for amino acids / proteins as there is nitrogen in all amino acid molecules (1 mark) Extra mark for correct use of the word legume or knowing these include peans + beans
62
# viral diseases Disease --> transmission --> Name of virus 1. Influenza (flu) 2. Common cold 3. Yellow Fever 4. Winter vomiting bug
**Influenza** (flu) --> coughs + sneezes (droplets) --> Influenza virus A or B **Common cold** --> coughs + sneezes (droplets) --> Rhinovirus **Yellow fever** --> Mosquitos --> Togavirus B **Winter vomiting bug** --> virus contaminated surfaces + food --> Norovirus
63
Phospholipid molecule? Phospholipid bilayer?
``` hydrophilic head - water 'loving' hydrophobic tail - water 'hating' ``` - Phospholipid bilayer - 2 layers of phospholipid molecules - Membranes are about 7-10 nm thick - There are proteins (carrier/channel) + glycoproteins (cell signaling) between phospholipids in the bilayer
64
What do phospholipid bilyaers do?
- Phospholipids are a barrier separating the outside + inside of the cell - with phospholipid **heads** facing the water in the cytoplasm or outside the cell - The **tails** are keeping away from water by all facing inwards. - **Protein** molecules can be receptors, ion channels, active transport, enzyme, electron carrier systems, carrier proteins - **Cholesterol** controls membrane fluidity - **Glycoproteins** – combination of a carbohydrate + a protein = example would be an antigen - **Antigen** used for cell recognition - antibodies produced in response to foreign antigens
65
Why's it called a fluid mosaic model
- Called a fluid mosaic model because molecules in membrane can move (useful for cell during cell division so daughter cells get some of all types of membrane molecules) - Called a mosaic because it looks like a mosaic floor
66
Passive v Active immunity
- Passive immunity is when you are given ready-made antibodies - Active immunity is when you are given a weakened form of the disease so you learn how to produce antibodies for the future
67
# movements through membranes Solid Liquid Gas
**Solid** – atoms or molecules close together in a fixed regular structure **Liquid** – atoms or molecules close together, but can move around each other **Gas** – atoms or molecules quite a long way apart, moving around at high speed, colliding with each other
68
Solute Solvent Solution
Solute is dissolved in a solvent to make a solution - **Solute** – solid - **Solvent** – a liquid. In biology solvents are usually water – used to dissolve a solute. - **Solution** – mixture of the solid and solvent. Sodium chloride (solute) + water (solvent) --> sodium chloride solution
69
Diffusion
- The movement of particles (molecules) from a place where they are in a high conc to a place where they are in a low conc due to the random movement of molecules - Diffusion evens out the distribution of molecules. - Diffusion occurs in a liquid and a gas. - Diffusion is faster in a gas than liquid (Leaves have air space in their spongy mesophyll because diffusion in gases is quicker than in the cytoplasm)
70
Brownian motion?
Brownian motion = looking at smoke particles floating in air using a microscope - The smoke particles move in a zig-zag pattern - The zig-zags are caused by air molecules colliding with the smoke particles = causing them to move + change direction - =shows how air molecules have a random movement
71
Osmosis
process by which water molecules move through a semipermeable membrane from an area of high water concentration to an area of low water concentration
72
Semi-permeable membrane, partially permeable membrane or selectively permeable membrane
- These all mean the same thing for osmosis] - A membrane with small holes (aquaporins) - Water molecules are small = can go through holes - Sucrose molecules (sugar) are large = cannot go through holes
73
Osmosis in animal cells
``` 1. Animal cell in water ``` - water enters cell (osmosis) from area of low solute conc to area of high solute conc through semi-permeable membrane - cell bursts = **cell lysis** ``` 2. Animal cell in concentrated salt solution ``` - water leaves the cell (low solute conc to high solute conc) - = **cell shrivells up**
74
Osmosis in a plant cell
``` 1. Plant cell in water ``` - **Cell is turgid**, has a high turgor pressure - = Cell membrane pushed against cell wall - Cell wall prevents bursting ``` 2. Plant cell in 1M sucrose Solution ``` - Water leaves the cell - cell membrane separates from cell wall = cell is said to be plasmolysed - =cell has low turgor pressure = **cell is flaccid**
75
Incipient plasmolysis?
- Incipient plasmolysis is when cell membrane is just starting to pull away from cell wall - Happens when concentration inside the cytoplasm + outside is about the same - = so **water enters + leaves at the same rate** - = No net movement of water molecules = movement of water in + out is in equilibrium
76
Examples of osmosis
- Jam – contains lots of sugar so water leaves bacterial cells and bacteria cannot destroy the jam. - Salt – food preservation - Salt – infection control – rub salt into a wound - In grown toenail - Plants exposed to salt – live near the sea – thick waxy cuticles and thick fleshy leaves. Wax reduces water loss and thick fleshy leaves reduces the surface area to reduce water loss. - Water uptake into plant roots is by osmosis. - Opening + closing of stomata uses osmosis. - Osmoregulation – excretory system – patient hydration
77
Saltmarsh?
A saltmarsh is a low lying area of vegetation on the coast, which is flooded by the sea up to twice per day The amount of flooding depending on the height of the tides which in turn depends on the position of the sun + moon
78
Adaptation of slatmarsh plants to being flooded with salty seawater a lot
Saltmarsh plants have to get water from the salty mud they are growing in as well as resist water loss from leaves which can be submerged in seawater twice per day = Consequently these plants have thick fleshy leaves (low surface area) with a waterproof waxy cuticle.
79
What is water potential? How can it explain osmosis?
- Water potential = ψw Pronounced Psi - Is a measure of pressure using units Pascals (Pa) or kPa - Water molecules exert pressure - Pure water has the maximum water potential which is 0 Pa - All solutions have lower water potentials than pure water, so negative values for water potential - Water always moves from a region of high water potential to low water potential **Osmosis is the movement of water molecules from a region of higher water potential to a region of lower water potential through a semi-permeable membrane**
80
Active transport
- The movement of molecules through a membrane + against a concentration gradient - Requires an input of energy, which usually comes from ATP (adenosine triphosphate). - Uses membrane carrier proteins
81
Examples of active transport How to check for active transport
- Absorption of amino acids from intestine into the blood. - Reabsorption of glucose in kidney (first convoluted tubule). - Sodium – potassium pump in nerves( exchange of Na+ + K+ to allow electrical conducting) ``` A way to check whether active transport is involved is to add a respiratory poison (eg cyanide) Cyanide prevents respiration and therefore prevents ATP production. If transport is stopped with cyanide then it is active transport. ```
82
hydrgen ion passing through membrane through active transport: (H+ - ATPase pump moves H+ ions against difussion gradient - EG kidney tubule cells make acidic urine)
- Carrier molecule binds to + hydrolyses ATP - making a 'high energy' complex - H+ ions binds to + combine with the 'high energy' complex - ATP attaches to carrier protein releasing energy and then ADP released - The energy causes the carrier protein to change shape, pumping the hydrogen ion through the membrane - Hydrogen ion released + carrier protein returns to original shape - The shape (conformation) change lowers affinity of carrier for H+. phosphat is lost + this induces another shape change back to original in step 1
83
Stomata
- tiny pores, mostly located on the underside of leaves - that facilitate gas exchange between the plant + the environment - They control the entry of CO2 for photosynthesis + the exit of O2 + water vapor (transpiration) - stomata is surrounded by guard cells and lower epidermis cells
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Facilitated diffusion
- Diffusion, but involves large protein molecules - Passive process that moves molecules across a cell membrane from high to low concentration with using proteins - Two types = carrier proteins + ion channels
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Facilitated diffusion through - carrier proteins
- carrier protein is within the phospholipid bilayer - Protein open from one side of membrane where conc is higher = molecule enters it = protein closes from that side and opens on other side = molecule exits on other side where conc is lower - movement down conc gradient - No input of energy - lets water molecules or small ions through quickly
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Facilitated diffusion through - Ion channels
- stimulus causes the "gate" to open or shut. - for diffusion of charged ions: Ca2+, Na+, K+, Cl- - Ions do not move easily through the non-polar lipid bilayer - One million ions per second can go through one ion channel - A gated ion channel is an ion channel that can open + close
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# macromolecules Proteins
**Proteins are polymers of amino acids, formed by long chains of amino acids joined together by peptide bond** - Only 20 amino acids are found in organisms.
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Examples of proteins' uses in living systems
1. **Structural proteins** - Keratin – hair - Collagen – tendons - Actin and myosis – muscles - Elastin - ligaments 2. **Transport** - Transport across membranes (ion channels etc) - Haemoglobin in transporting oxygen 3. **Enzymes** - Digestive enzymes - Enzymes involved in metabolism 4. **Hormones** - Protein hormones - eg Insulin - (some hormones are made from steroids such as testosterone = not protein) 5. **Antibodies** - Defense against diseases - eg antibodies for covid-19
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Proteins can combine with other molecules: 1. Glycoprotein? 2. Lipoprotein? 3. Metalloprotein?
- **Glycoprotein** = combination of protein + carbohydrates (eg mucus) - **Lipoprotein** = combination of a protein + a lipid - **Metalloprotein** = combination of a metal + a protein (eg haemoglobin, which contains iron)
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Structure of amino acids
- contain **Amino group** (NH3) - Contain **carboxylic acid group** (COOH) - contain **R group** or seen as 'H' - Amino acids are different from each other because they have a different R-group - EG: A single hydrogen in the R-group = is glycine - EG: CH3 in the R-group = Alanine
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What is the difference between a polypeptide and a protein?
answer it is not very clear - A short chain of amino acids is a polypeptide - whereas a long or folded chain or two or more chains of amino acids is a protein
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Two amino acids bond together to make a...
- Two amino acids bond together to make a **dipeptide** - Water is released so this is a **condensation reaction** - The bond formed is called a **peptide bond** (forms between a NH2 + COOH group - There is still an amino acid at one end + a carboxylic acid group at the other end so the molecule can continue to grow in length
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1. Dipeptide? 2. Tripeptide? 3. Polypeptide?
- **Dipeptide** = two amino acids bonded together by a peptide bond. - **Tripeptide** = three amino acids bonded together by peptide bonds. - **Polypeptide** = a chain of amino acids up to about 50 amino acids. A polypeptide is a protein, but many proteins (e.g. insulin) are far too large and complex to be called polypeptides.
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Polarised vs unpolarised light
- light travels as a wave **Unpolarised light** - the electric field vectors are randomly oriented - = causing vibrations in multiple directions (sunlight, incandescent bulbs, halogen lighting) - Light waves that reflect in more than one place/direction **Polarised light** - The electric field vectors are aligned in a single plane - = resulting in vibrations in one direction (A laser) - polarized light waves are those that reflect in a single place/direction - - shine a beam of light (unpolarised) through a polarizer (polarising filter) = light becomes polarised - Polarising sunglasses completely cut out reflections = because reflected light is also polarised
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Polarised light can be rotated Whats it called when polarised light is rotated to the right? vs to the left?
- **Dextrorotation** = rotating polarised light to the right (clockwise) -EG D-alanine - **Laevorotation** (/ levorotation) = rotating polarised light to the left (counterclockwise) -EG L-alanine.
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Stereoisomers of amino acids (mirror image) - Optical isomers
Central carbon bonded to four different groups. Asymetric. - Stereoisomers of amino acids are non-superimposable mirror images of each other that exhibit optical isomerism
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What are the 2 forms of stereoisomers of amino acids?
All amino acids except glycine have stereoisomers, which are compounds that exist in two forms: L-and D- - The **L-form** (Laevo) is left-handed - The **D-form** (Dextro) is right-handed - EG L-alanine has the CH3 on the left side + NH2 on the right side, but D-alanine has the CH3 on the right side + NH2 on the left side (both have COOH at the top and H at the bottom, with a central C) | see drawing
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pH scale
1 - 14 ``` 1- strong acid 3 - 6 - weak acid ``` ```7- neutral``` ``` 8 - 13 - weak alkali 14 - strong alkali ```
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logarithmic ph scale?
**logarithmic** ph scale = - for ech 1 pH change towards 1 = there is10x the amount of hydrogen present as the pH before that eg if there were 20 hydrogens at pH 5, then at pH 4 there will be 200 hydrogens.
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Ocean acidification:
- Increased carbon dioxide in the atmosphere dissolves in seawater to create carbonic acid - = This reduces availability of calcium carbonate making it difficult for organisms (eg corals + molluscs) to incorporate calcium carbonate into their shells - coral growth is already slowing = suggest will stop by the year 2035 + corals start to dissolve by 2060
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pH affects amino acids
- at low pH, the amino acid has more hydrogens - A zwitterion is a molecule with an equal number of positively and negatively charged functional groups - amino acid common example - Amino acids act as buffers (a chemical that prevents / reduces pH change) - as pH changes structure of amino acid, it will also change structure of protein - enzymes are sensitive to pH
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Disulphide bridge
- S-S bonds - They are covalent links between the Sulphur atoms of two cysteine amino acids - Can only be formed between 2 cysteine molecules as these are the only amino acids containing sulphur - important for the stability + proper folding of proteins in tertiary structure - Disulphide bridges are found in insulin.
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Disulphide brideges in insulin
- disulphide bridge hold the 2 chains (A chain + B chain ) together in an insulin molecule - A chain- 21 amino acids = 5 amino acids, 2 cysteine, 8 amino acids, cysteine, amino acid - B chain- 30 = 6 amino acids, cysteine, 11 amino acids, cysteine, 11 amino acids
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Hydrogen bonds in water, in proteins, and in amino acids
- **water**: Hydrogen bonds are very important because they mean water is a liquid at the temperature range at which biomolecules function. Forms between partial negative O- and partial positive H+
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Hydrogen bonds in proteins and amino acids
- **Protein**: H bonds form between 2 polypeptides (or parts of the same polypeptide or protein) - Hydrogen bond between the δ+ H from NH2 and the δ- O from COOH of another amino acid - **Amino acid**: Hydrogen bonds can hold a chain of amino acids together in a helix. - EG- Keratin is a protein found in hair + the helical structure combined with hydrogen bonds makes hair stretchy
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Structure of a protein?
**Primary structure** = the order / sequence of amino acids in a protein. **Secondary structure** = Folding of protein into alpha helix (in keratin) or beta pleated sheet **Tertiary structure** = the 3D shape of a protein results from bonds between distant parts of a chain = causing the chain to fold. **Quaternary structure** = the relative positioning of two or more polypeptide chains associated in one protein. There is no covalent bonding between these chains??. Held together by hydrogen bonds, van der Waals bonds, london dispersion forces, disulphide bridges, electrostatic forces
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# cell division Haploid v diploid
- Chromosomes are normally in pairs. - A **human body cell** has 23 pairs of homologous chromosomes = **46** chromosomes = **diploid number** (2n) - **Gametes** have half this number of chromosomes = are **haploid** (n) = **23** = chromosomes in gamete are not in pairs - A gamete must have half the normal diploid number, so that fertilisation results in the zygote having the normal diploid number of chromosomes. **Fertilisation > 23 + 23 = 46** Sperm + Egg = Zygote Gametes = sperm + eggs. Zygote = fertilised egg
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# cell division What are the stages on cell division?
A) Interphase B) Early prophase C) Late prophase D) Early metaphase E) Late metaphase F) Early anaphase G) Late anaphase H) Early telophase I) Late telophase
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A) Interphase B) Early prophase C) Late prophase
**A) Interphase** - cell has normal appearance of non-dividing cell condition: chromosomes too threadlike for clear visibility - cell grows + prepares for division by replicating its DNA + organelles **B) Early prophase** - Chromosomes become visible as they contract + nucleulos shrinks - centrioles at opposite sides of the nucleus - spindle fibres start to form **C) Late prophase** - Chromosomes become shorter + fatter - each seen to consist of a pair chromatids joined at the centromere - Nucleolus disappears - Prophase ends with breakdown of nucleus membrane
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D) Early metaphase E) Late metaphase
**D) Early metaphase** - Chromosomes arrange themselves on equator of spindle - homologous chromosomes do not associate **E) Late metaphase** - Chromatids draw apart at the centromere region - the chromatids of each chromosome are orientated towards opposite poles of the spindle
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F) Early anaphase G) Late anaphase
**F) Early anaphase** - Chromatids part company + migrate to opposite poles of cell - he centromeres leading **G) Late anaphase** - Chromosomes reach their destination on opposite poles
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H) Early telophase I) Late telophase
**H) Early telophase** - The cell starts to constrict across the middle **I) Late telophase** - Constriction continues - Nucleur membrane + nucleolus reformed in each daughter cell - spindle apparatus degenerates - Chromosomes eventually regain their threadlike form + the cells return to resting condition (interphase) - the diploid daughter cells are idntical to original parents cell (have precisely the same chromosome constitution)
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Stages of meiosis
A) Interphase B) Early prophase 1 C) Mid prophase 1 D) Late prophase 1 E) Metaphase 1 F) Anaphase 1 G) Telophase 1 H) Prophase 2 I) Metaphase 2 J) Anaphase 2 K) Telophase 2
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A) Interphase B) Early prophase 1 C) Mid prophase 1 D) Late prophase 1
**A) Interphase** - Cell in normal non-dividing conditions with chromosomes long + threadlike **B) Early prophase 1** - Chromosomes contract, becoming more clearly visible - Nucleolus shrinks **C) Mid prophase 1** - Homologous chromosomes come together (synapsis) forming a bivalent **D) Late prophase 1** - Each chromosome seem to consist of a pair of chromatids
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E) Metaphase 1 F) Anaphase 1 G) Telophase 1
**E) Metaphase 1** - Chromosomes arrange themselves on equator of spindle **F) Anaphase 1** - Homologous chromosomes part company + migrate to opposite poles of the cell **G) Telophase 1** - The chromosomes have reached their destination + the cell constricts across middle (same as mitosis)
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H) Prophase 2 I) Metaphase 2
**H) Prophase 2** - The 2 daughter cells prepare for the second meitotic division: centrioles have replicated + a new spindle is formed **I) Metaphase 2** - Chromosomes arrange themselves on the spindle
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J) Anaphase 2 K) Telophase 2
**J) Anaphase 2** - Chromatids part company + migrate to opposite poles of the cell **K) Telophase 2** - Cell constricts across the middle + the nucleur membranes + nucleoli are reformes (same as end of mitosis) - Chromosomes regain their threadlike form + the cells go into the resting state (interphase) - the haploid daughter cells have half the number of chromosomes as the original parent cell
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Enzymes
- biological catalysts - A catalysts - a chemical that speeds up a reaction without being used up. - They speed up reaction by providing alternative reaction pathway with lower activation energy - = catalyst can be used many times over a long period of time An example of a catalysts is the catalytic converter in a car exhaust system. It converts carbon monoxide to carbon dioxide, breaks down waste hydrocarbons + also reduces the emissions of nitrogen oxides.
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Enzyme naming? Which substrate do these enzymes work on + what's the products?
Enzyme naming -usually named after the substrate with the latters 'ase' at the end Substrate --> Enzyme --> Products Starch --> **Amylase** --> maltose Maltose --> **Maltase** --> glucose Lipid --> **Lipase** --> Fatty acids + glycerol Proteins --> **pepsin / protease** --> polypeptides + amino acids Polypeptide --> **Trypsin** --> amino acids Hydrogen peroxide --> **Catalase** --> water + oxygen
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Enzymes + temperature
- Enzymes are made from globular proteins. - Enzymes are denatured by high temperatures. - = greater than 40°C = part of the reason that human body temperature is 37°C. Body temperature is just below the temperature at which enzymes would be denatured. - Fever, heat stroke can put a human body temp above 37°C = is potentially dangerous
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Catalase enzyme [catalase = assessed lab]
- Catalase found in yeast cells, potato + liver. - catalyses- Hydrogen peroxide --> oxygen + water 2H2O2 --> O2 + 2H2O - Catalase has one of the fastest turnover numbers known = 6000000 - Turnover number = number of molecules one molecule of enzyme will break down per minute.
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Temperature + catalase lab method [assessed lab]
1. test tube 1 - 1cm3 yeast suspension test tube 2 - 2cm3 hydrogen peroxide + washing liquid 2. Put test tubes in water bath for 5 minutes 3. then add hydrogen peroxide to yeast + Wait 30 seconds - = will produce froth = bubbles of oxygen (as O2 is a product) - = measure the 'froth height' - froth height is direclty proportional to rate of reaction
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How does the froth height (=Rate of reaction) change with temperature
- Temperature quotient. Q10 = 2 - = between 0- optimum temp (=40°C for catalase) everytime temp increases by 10°C, the reaction rate doubles - until it reaches the optimum temp = after that ROR will drop to 0 as enzyme denatures
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Poikilotherms? homeotherms?
**Poikilotherms** - cold blooded organisms **homeotherms** - warm blooded organisms
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Enzymes + pH
- Enzymes have an optimum pH = the pH they work fastest at - extreme pH = denature = active site shape changed - Pepsin – found in the stomach where there is hydrochloric acid about pH 1-2. - Trypsin – found in the small intestine pH 8.5
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Enzymes turnover number?
- the number of substrate molecules that 1 molecule of enzymes convert into products pr minute - catalase is one of the fastest enzymes = turnover value of 6 million
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Lock + Key model vs induced fit model
- substrate binds to specific active site on enzyme (specifity - enzyme will only work on 1 substrate) - enzyme-substrate complex - enzyme catalyses reaction + converts it to products - enzyme is free to find another substrate molecule `INDUCED FIT MODEL - enzyme changes shape slightly to fit substrate`
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Enzyme inhibitors?
- chemicals that slow/ stop an enzyme from working - can temporarily or permanently stop an enzyme from working -enzyme inhibitors may include poisons we've heard of... - arsenic - mercury - sulphonamine drugs - sarin - cyanide - curare
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Competetive inhibitors (reversible)
- doesn't bind permanently to active site - it **FLOATS** in an active site - it floats in + out of active site competing with substrates = slows the enzyme down but doesn't stop it working
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Non-competitive inhibitors (irreversible)
- inhibitor molecule fits permanently into the **allosteric site** = this permanently changes the shape of the enzyme molecule =active site loses specific shape = doesn't work again since cant bind to substrate Allosteric site = a binding site on an enzyme that is separate from the active site
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rate of enzyme reaction graphs with the different enzyme inhibitors
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# **Lipids** - biological molecules made of carbon, hydrogen + oxygen Triglyceride Lipid
- One glycerol molcule bonded to 3 fatty acids - through ester bonds in condensation reaction - 3 molecules of water (H2O) are produced when ester linkage forms (glycerol molecule down the side is hydrocarbon chain but on the right side of it its -OH = the H from this O-H is what bonds with the OH from the COOH of the 3 fatty accids...dont have to draw whole carbon chain out for them just the carboxylic acid group bonded to -R1, R2, R3)
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Saturated VS Unsaturated fatty acids
- both consist of a hydrocarbon chain with carboxylic acid on the end of the chain **Saturated**: - lipids which **dont contain any C=C double bonds** - = has full number of H atoms [found in animal fats] **Unsaturated**: - lipids which **contain C=C double bonds** in carbon chain - = it does not have the full number of hydrogen atoms [found in plants] - The double bond causes a bend in the carbon chain
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What does the length of the carbon chain determine?
Length of the carbon chain determines the **type of fatty acid**. Examples: 1. *Stearic acid*: CH3(CH2)16 COOH 2. *Palmitic acid*: CH3(CH2)14 COOH
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Phospholipid
- Found in cell membranes – fluid mosaic model - **Polar head** – contains a negatively charged phosphate group = hydrophilic (water loving) - **Non-polar tail** – is hydrophobic (water hating) fatty acids Phospholipid Molecular Structure = Carbon chains will be longer than shown + can contain double bonds, which form ‘kinks’. [SEARCH ON GOOGLE TO SEE STRUCTURE]
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# Carbohydrates know the structure of a glucose molecule + difference between alpha + beta glucose
* carbon atoms labelled in clockwise * a glucose has H ontop and OH under * B glucose has OH ontop and H under
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# disacharides Maltose? Lactose? Sucrose?
glucose + glucose –> maltose glucose + galactose –> lactose glucose + fructose –> sucrose
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starch, cellulose, glycogen are polysacharides Why is starch is converted to glucose in humans
- **starch** - made of a-glucose (mix of 2 polysacharides: amylose + amylopectin) - **cellulose** - made of b-glucose = we cant digest - **glycogen** - a-glucose - food store in animals **starch** --> **maltose** (by amylase in mouth + dulodenum) --> **glucose** (maltase in ileum of small intestine) - starch is digested to reduce the molecule to a size that can pass through semi-permeable membrane - gut wall
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A Tetrose? A Pentose? A Hexose?
A Tetrose - a **4** carbon monosacharide A Pentose - a **5** carbon monosacharide A Hexose - a **6** carbon monosacharide [glucose]
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Bonding between polysacharides?
* glycosidic links/bonds form by glycosidic condensation between 2 chains of glucose molecules between C1 + C6 * The same type of reaction bonds glucose molecules into their chain between C1 + C4
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1. Starch
A storage polysacharide in plants made of a amylose + amylopectin **Amylose** (approx 20%) - linear chain of a-glucose molecules joined by 1-4 glycosidic bonds (same as maltose) - adopts a helical structure due to the intramolecular arrangments of bonds in carbon **Amylopectin** (approx 80%) - chain of a-glucose molecules joined by 1-4 glycosidic bonds - with branching formed by 1-6 glycosidic bonds
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2. Glycogen
main energy storage polysacharide in animals - Chain of **a-glucose** molecules joined by **1-4** glycosidic bonds - with branching formed by **1-6** glycosidic bonds - even **more branching** than amylopetin but same structure
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3. Cellulose
Structural polysacharide in plants * linear chain of B-glucose joined by 1-4 glycosidic bonds * cellulose froms straight chains + is the basis of plant fibre