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Summary Biology Topic 7 A-level notes

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Notes on all of topic 7 for Biology Edexcel A level paper 2 on 17/06/22. Written as bullet points and covers the whole topic.

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Topic 7 notes
Joints:

 In a synovial joint, the bones that move are separated by a cavity filled with synovial fluid, which
enables them to move freely
 Bones are held in position by ligaments to control and restrict the amount of movement in the joint
 Tendons join muscle to bones, enabling muscles to power joint movement
 Tendon = muscle to bone
 Ligament = bone to bone, strong and flexible
 Synovial membrane – secretes synovial fluid
 Synovial fluid – acts as a lubricant
 Cartilage – absorbs synovial fluid, acts as a shock absorber
 Pads of cartilage – additional protection
 Fibrous capsule – encloses joints

Muscle:

 Muscle - made up of muscle fibres
 Muscle fibre – single muscle cell surrounded by cell surface membrane
 Myofibril – numerous inside a muscle fibre
 Sarcomere – a repeated unit that makes up a myofibril, made up of actin (thin filament) and myosin
(thick filament)

Sliding filament theory:

 Actin molecules are associated with protein molecules troponin and tropomyosin
 When nerve impulses arrive at a neuromuscular junction, calcium ions are released from the
sarcoplasmic reticulum
 Calcium ions diffuse through the sarcoplasm to initiate the movement of the protein filaments:
 Calcium ion attaches to the troponin molecule, causing it to move
 Tropomyosin on actin filament shifts its position, exposing myosin-binding sites on the actin filaments
 Myosin heads bind with myosin-binding sites on the actin filament, forming cross-bridges
 When myosin heads bind to actin, ADP and Pi on myosin heads are released
 Myosin changes shape, causing head to nod forward, the movement results in the relative movement
of the filaments, attached actin moves over the myosin
 An ATP molecule binds to the myosin head, this causes the myosin head to detach from the actin
 An ATPase on myosin head hydrolyses ATP to form ADP and Pi
 This hydrolysis causes a change in shape of the myosin head, so it returns to its upright position,
enables cycle to start again
 Collective bending of many myosin heads combines to move actin filament relative to the myosin
filament = muscle contraction

Carbohydrate oxidation:

 Glucose oxidised to release energy
 Input energy needed to break bonds in glucose and water is not as large as energy release when
bonds in carbon dioxide and water are formed, so there’s an overall release of energy
 Glucose and oxygen aren’t directly brought together, this would release large amount of energy
which would be damaging to the cell
 Glucose is split in a series of small reactions controlled by a specific intracellular enzyme




Glycolysis:

,  Stores of glycogen from muscle or liver cells must be converted to glucose (main respiratory
substance)
 Glucose is stable and unreactive, so an input of energy from ATP is needed to start the process
 2 phosphate groups are added to glucose from 2 ATP to increases reactivity of glucose – energy
released from reaction
 Energy can be used in regeneration of ATP, this is substrate level phosphorylation as energy comes
from substrates
 This is now split into 2 x phosphorylated 3C compound, each oxidised to pyruvate
 2 hydrogens removed here are taken up by coenzyme NAD producing a reduced coenzyme

Link reaction:

 Pyruvate is decarboxylated - carbon dioxide released as a waste product
 Pyruvate is dehydrogenated – 2 hydrogens removed and taken up by coenzyme NAD
 Results in a 2C compound which combines with coenzyme A = acetyl CoA
 CoA carries the 2C acetyl group into Krebs cycle

Krebs cycle:

 Each 2C acetyl CoA combines with a 4C to create a 6C compound
 6C undergoes decarboxylation and dehydrogenation = CO2 and 2H, hydrogen combines with NAD to
reduced it
 5C compound then undergoes carboxylation = CO2, substrate level phosphorylation = ATP,
dehydrogenation = 6H to reduce 2NAD and an FAD
 Overall products of Krebs = 2CO2, ATP, 3NADH, FADH

Electron transport chain:

 Reduced coenzymes shuttle hydrogen atoms to the electron transport chain on the mitochondrial
inner membrane
 Each hydrogen’s electron and proton separate, electron passes along a chain of electron carriers
 Energy released as electrons pass down the chain
 Energy used to move hydrogen ions from the matrix across the inner mitochondrial membrane into
the intermembrane space = steep electrochemical gradient across inner membrane
 There’s a large difference in concentration of hydrogen ions across membrane and a large electrical
difference so the intermembrane space is more positive than matrix
 Hydrogen ions diffuse down this electrochemical gradient through hollow protein channels situated in
ATP synthase (stalked particle) embedded and protruding from the inner mitochondrial membrane
 As H ions pass through channel, ATP synthesis is catalysed by ATP synthase as H ions have causes a
conformational change in enzyme’s active site, enabling ADP and Pi to bind to the site
 Within the matrix, hydrogen ions and electron recombine to form hydrogen atoms, these combine
with oxygen to form water molecules
 Oxygen is the final electron acceptor
 This method of ATP synthesis is oxidative phosphorylation
 Amount of ATP produced depends on efficiency, and some hydrogen ions are used to exchange ADP
and ATP across membrane which used up hydrogen ions, so less hydrogen ions available for
generation of ATP

Rate of respiration:

 Rate of aerobic respiration can be determined by measuring uptake of oxygen using a respirometer
 As respiration is a series of enzyme catalysed reactions, its rate will be affected by concentration of
enzyme and substrate, by temperature and pH
 Concentration of ATP in a cell will also control rate
 ATP inhibits the enzyme in the first step of glycolysis
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