Sem 1 Flashcards

1
Q

Features of competitive inhibitors

A
  • structural resemblance to substrate
  • no reaction but blocks substrate from entering active site
  • can be reversed by an increase in [s]
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2
Q

Features of non-competitive inhibitors

A
  • allosteric site
  • changes shape of active site
  • substrate is blocked from entering
  • can no be reversed by increasing [s]
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3
Q

Structure of CNS

A

Made up of brain and spinal cord :

Frontal lobe - reasoning, planning, movement, emotion and problem solving
Occipital lobe - processing visual information
Temporal lobe - perception and recognition of sounds, memory and speech

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4
Q

Function of CNS

A

Receives and processes information and coordinates organ function

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5
Q

Function of peripheral nervous system

A

Sends information from organs eg blood pressure , fullness of stomach into the CNS
(Connects the CNS to the organs, limbs and skin)

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6
Q

Somatic nervous system

A

Regulate contraction of skeletal muscle - voluntary

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7
Q

Autonomic nervous system

A

Regulate function of internal organs - involuntary

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8
Q

Structure of neurons

A

Cell body - organelles which carry out cellular functions eg protein synthesis, energy production

Dendrites - receive input from other neurons via synapses

Axon - nerve fibre transmits action potential towards postsynaptic neuron or the effector organ

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9
Q

What are the 5 phases of an action potential

A
1- resting potential 
2-threshold 
3-rising phase
4-falling phase 
5-recover phase 
  • action potential arise from a change in membrane potential
  • ions move down an electrochemical gradient
  • movement of NA+ and K+ results in an action potential
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10
Q

3 Amine neurotransmitters and their functions

A

Serotonin - influences mood
Dopamine - reward pathway
Acetylcholine - CNS neuromuscular function

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11
Q

Main functions of the ER

A
  • translocation of proteins
  • glycosylation of proteins
  • assembly of lipids
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12
Q

Lysosome function in cellular digestion

A
  • fuse with food vacuoles
  • polymers digested into monomers
  • pass to cytoskeleton to become nutrients of cell
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13
Q

what is Apoptosis

A

Auto-destruction process where lysosome break open and kill cell

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14
Q

Main functions of Golgi body

A
  1. Protein modification
  2. protein processing
  3. protein sorting and localization
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15
Q

3 stages of converting food energy into ATP (mitochondria)

A

Stage 1.
Large molecules broken down into smaller subunits

Stage 2.
Numerous small molecules converted to a few molecules which play a central role in metabolism

Stage 3.
Oxidation to produce ATP

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16
Q

Mitochondrial ATP synthesis

A
  1. The energy from the high energy electrons is used to pump protons across the inner mitochondrial membrane from the matrix and into the inter membrane space
  2. The protons then flow back down the gradient and this energy dribbles coupled ATP synthesis
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17
Q

Function of cytoskeleton

A

Provides a supporting framework for the cell and gives the cell its particular shape
Cytoskeleton and its associated motor proteins organisms and moves the cytoplasmic contents

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18
Q

what are the 2 types of stroke

A
  • ischemic stroke (most common)

- hemorrhagic stroke

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19
Q

Causes of an ischemic stroke

A
  • Blood vessels occluded (clot or plaque)

- lack of nutrients, o2 , cell death

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20
Q

Where are the 2 regions of a stroke

A
  1. umbra- centre

2. penumbra - periphery

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21
Q

Treatment of ischemic stroke

A

Tissue-type plasminogen activator (alteplase)

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22
Q

Treatment of hemorrhagic stroke

A

Surgery in order to remove the clot

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23
Q

Cause of Parkinson’s disease

A

Idiopathic - don’t know the exact cause

Dopaminergic neurons - loss of these neurons that produce dopamine

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24
Q

Affects of Parkinson’s disease

A

Dopamine coordinates fine movement so a loss of dopamine results in tremors -uncontrolled movement

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25
Q

Treatment of Parkinson’s disease

A

Cannot simply use dopamine because it can’t cross the brain cloud barriers so levodopa which looks very similar is used

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26
Q

Cause of Alzheimer’s disease

A

Caused by the abnormal build-up of proteins in and around brain cells

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27
Q

Treatment of Alzheimer’s disease

A

No affective medicine for the disease itself so treatment is focused on symptoms

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28
Q

Function of GABA

A

Main inhibitory neurotransmitter in CNS.

Binding of GABA to receptor inhibits transmission of an action potential

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29
Q

What is hyperpolarization

A

Accumulation of negative charge inside neuron

NA+ channels don’t open, no influx of NA+ so no transmission of action potential

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30
Q

Causes of schizophrenia

A

Excessive neurotransmission (action potentials) caused by dopamine

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31
Q

Treatment of schizophrenia

A

Treated with antipsychotics -

Bind to dopamine receptors - reduces action potentials, reduces neuronal activity in the brain , reduces anxiety

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32
Q

Function of the GI system

A
  • digestion of food
  • absorption of nutrients, and drugs
  • Elimination
  • mechanical and chemical breakdown of food
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33
Q

4 regions of the GI tract

A

Mouth - breaks up food particles

Esophagus - transport of food to stomach via sphincter

Stomach - secretion of gastric juices for chemical digestion

Small intestines

34
Q

4 accessory organs

A
  • salivary gland
  • liver
  • gallbladder
  • pancreas
35
Q

Role of gastric juices in food and drug absorption

A

HCI (controlled by vagus nerve and hormone gastrin) and digestives enzymes -> initiate s the digestion of proteins

36
Q

Role of mucus coating in food and drug absorption

A

Lubricates and protects epithelial surfaces

37
Q

Role of gastric emptying in food and drug absorption

A

Moves food in the stomach to small intestine

38
Q

Features of the small intestine

A
  • large surface are and high perfusion
  • exposure to enzymes and solubilizes
  • receives secretion from liver and pancreas
39
Q

Why is large surface area so important for drug absorption after oral administration

A

Dissolved drugs absorbed here

40
Q

Main role of the liver in digestion

A
  • Main site of metabolisms xenobiotics
  • secretes bile
  • stored in gallbladder between meals
  • important for digestion of lipids
41
Q

Role of pancreas in digestion

A
  • proteolytic enzymes
  • lipase for digestion of lipids
  • HCO3 stomach acid neutralizing
42
Q

Digesting carbohydrates

A

Starch (amylase) -> disaccharide -> monosaccharide - transported across intestinal epithelium into blood

43
Q

Digestion of proteins

A

Peptide (pepsin) -> peptide fragments -> amino acids - active transport to epithelial cells

44
Q

Digestion of lipids

A

Emulsification ( bile salts, pancreatic lipase , Michelle formation - transport of lipids — completed in small intestine )

45
Q

Role of large intestine in absorption

A
  • Reabsorption of water and salts from chyme
  • Absorption of drugs minimal compared to small intestine
  • mixing and propulsion of contents
  • indigestible residue and liquid eliminated as facial waste
46
Q

Anatomy of the gut

A

Caecum -> ascending colon -> transverse colon -> descending colon -> sigmoid

47
Q

Sign and symptoms of IBS

A

Symptoms include stomach cramps, bloating, diarrhea and constipation. These come and go and can last for days, weeks or months at a time. Usually a lifelong problem with no cure.

48
Q

Treatment for IBS

A
  • change to diet or lifestyle
  • IBS friendly diet - low FODMAP diet
  • exercise and reducing stress
  • probiotics
49
Q

Two main forms of IBD

A
  • Ulcerative colitis - inflammatory disease that affects the mucus a of the colon and rectum
  • Crohn’s disease - inflammatory disease that affects the gut (Small and large intestine)
50
Q

Signs and symptoms of IBD

A
  • diarrhea sometimes mixed with food, mucus and pus
  • cramping
  • malaise fever
  • loss of appetite and weight
51
Q

Treatment of IBD

A
  • antibiotics
  • corticosteroids
  • biologics
52
Q

3 stages of protein synthesis

A
  1. initiation
  2. elongation
  3. termination
53
Q

Protein synthesis: initiation

A

Small subunit complexes with initiation factors and base parings occurs - start codon of mRNA is positioned in the ribosomal P site and tRNA joins

54
Q

Protein synthesis: elongation

A

The ribosome has 3 sites where tRNA can bind:
The A site, P site and E site.
Only 2 of these are occupied at one time.
The ribosome moves 1 codon towards the end of the mRNA so that the growing peptide chain moves from the A to the P site. This means that unloaded tRNA moves to the E site. The A site is now empty -> then it all happens again

55
Q

Protein synthesis: termination

A

-synthesis continues until a stop codon is reached (UAA, UGA OR UAG)

56
Q

3 ways antibiotics block bacterial ribosomes

A
  • inhibition of initiation
  • prevention of tRNA binding to the A site
  • blocking the exit tunnel
57
Q

Tetracycline

A

Prevents tRNA binding to the A site - most common current use is in the treatment of severe acne

58
Q

Chloramphenicol

A

Inhibition of peptide bond formation

59
Q

Erythromycin

A

Blocking the exit tunnel of the ribosome

60
Q

What is PTM

A

Post-translational modification:

The enzymatic modification of a protein after its translation

61
Q

5 types of PTM

A
  1. Lipidation
  2. phosphorylation
  3. Glycosylation
  4. Acetylation
  5. methylation
62
Q

Alpha helix features

A
  • R group extend on the outside
  • one complete turn every 3.6 amino acids
  • twists clockwise
63
Q

Amphipathic helix

A

Helix with hydrophilic and hydrophobic faces.
Amphipathic helixes posses hydrophilic amino acids on one side and hydrophobic residues on the other; such alpha helices in some case can be used to associate a protein or peptide to a membrane

64
Q

Complex helices

A

Alpha helices can wind around each other to form “coiled-coils”

65
Q

Features of a beta sheet

A
  • R group point up and down
  • Strands held by H bonds between backbone
  • H bonds connect an amino acid in one chain with two from another chain
66
Q

Turns and bends in secondary structure

A

Turns and bends used to change direction in which sheets or helices run

67
Q

Loops and turns - protein tertiary structure

A

Found on protein surfaces controls the size and shape:

Loops - contains stretches of hydrophilic residues thus found on surfaces of proteins. Used to connect alpha helixes and beta sheets

Turns - same as loop but with less than 5 residues

68
Q

Structure of lipid bilayer

A

Made up of two layers of phospholipids that are amphipathic compounds. Phospholipid molecule are arranged into two layers form a lipid bilateral

69
Q

Function of cholesterol in bilayer

A

Present in the space among the hydrophobic tails of phospholipids in the lipid bilayer to regulate the fluidity of the cell membrane. The role of cholesterol is temperature dependent. At high temperatures, it decreases the mobility of phospholipid molecules while at a lower temperature, it promotes their mobility

70
Q

Function of glycolipids

A

Glycolipids serve to stabilise the cell membrane. They’re are also responsible for cell to cell interactions. Some also serve as cell surface receptors

71
Q

What are transmembrane proteins

A

A transmembrane protein has the following structure:

  • A hydrophilic domain that interacts with the molecules present in the cytoplasm of the cell
  • A hydrophobic domain that is responsible for anchoring the protein in the cell membrane
  • another hydrophilic domain that interact with molecules in the surrounding environment of the cell
72
Q

Anchored proteins

A

Proteins that are not in contact with the cell membrane. Attached to a lipid residue that is inserted into the lipid belayer of the cell membrane. Present either in the cytoplasm or in the extracellular fluid

73
Q

Peripheral proteins

A

Proteins that are present on one side of the cell membrane. These are temporary proteins and lose their association with the cell membrane as soon as they have preformed their function

74
Q

Carbohydrates in the lipid bilayer

A

They are involved in cell to cell recognition and other inter-cellular interactions

75
Q

Cell membrane anchoring the cytoskeleton

A

Cytoskeleton is anchored to the the cell membrane via linker proteins such as integrin. Kept anchored to the cell membrane vials these anchoring proteins

76
Q

Cell membrane and cell to cell recognition

A

This function is preformed by glycolipids and glycoproteins present on the outer surface of cell membranes -> can be recognised by partner cells but not by the cells of the other tissues

77
Q

Endocytosis

A

The membrane of the cell extends around the large substance to form an endocytic vehicle. This vehicle is later taken in by the cell as it breaks from the cell membrane.

78
Q

Exocytosis

A

The preformed vesicles fuse the cytoplasmic surface of the cell membrane. The vehicle becomes a part of the membrane while the substance is dumped into the extra cellular fluid

79
Q

Active transport proteins

A

Two main families of transport proteins use ATP hydrolysis to pump molecules across membranes

  1. P class transporters (ion pumps)
  2. ABC transporters
80
Q

ABC transporters

A

Called abc because they contain two highly conserved ATP-Binding-Cassettes
Used for export in eukaryotes