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Pharm Y1 > Patient Semester 1 > Flashcards

Patient Semester 1 Flashcards

1
Q

What is the diameter of a prokaryotic cell?

A

1-5um

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2
Q

What is the diameter of a eukaryotic cell?

A

10-100um

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3
Q

What is the thickness of a membrane?

A

6-10nm

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4
Q

Define amphipathic.

A

Both hydrophilic and hydrophobic

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5
Q

What is the glycocalyx?

A

The layer of carbohydrate on a cell membrane

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6
Q

What three methods are used to move small molecules?

A

Simple diffusion
Facilitated diffusion
Active transport

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7
Q

What is the diameter of an LDL molecule?

A

22nm

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8
Q

What is the diameter of an HDL molecule?

A

7-12nm

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9
Q

By what method are large molecules transported across membranes?

A

Vesiculation

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10
Q

What are the three types of lipid?

A

Simple- made up of glycerol and fatty acids
Complex- other groups such as sugars or phosphates attached
Sterols- heterocyclic

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11
Q

What is the width of a DNA alpha helix?

A

2nm

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12
Q

What is the length of one turn in a DNA alpha helix?

A

3-4nm

10 base pairs

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13
Q

In what direction are nucleic acids written?

A

5’ to 3’

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14
Q

What does antiparallel mean?

A

Moving in opposite directions

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15
Q

At what rate does DNA replication occur?

A

Occurs at approximately 1000 bases per second

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16
Q

What do topoisomerases do?

A

Type I- cuts one DNA strand, relaxation occurs, the strand is then reattached
Type II- cute both DNA strands, passes another unbroken helix through it and then rejoins the strands

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17
Q

What is the leading strand?

A

It is the strand of DNA that is made continuously, moving toward the 3’ end and the replication fork

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18
Q

What is the lagging strand?

A

The strand of DNA which is made in short fragments which are subsequently joined together

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19
Q

What primes DNA synthesis?

A

A short strand of RNA with a free 3’OH group produced by primase

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20
Q

When complete, what enzyme removes the RNA primer?

A

DNA polymerase I

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21
Q

What antibiotics inhibit bacterial DNA gyrases and topoisomerase IV?

A

Fluoroquinolones

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22
Q

Which antibiotic preferentially inhibits bacterial RNA polymerase?

A

Rifampicin

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23
Q

Which viruses make DNA from RNA? Using what enzyme?

A

HIV and HSV using reverse transcriptase

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24
Q

What is removed from pre mRNA using spliceosomes?

A

Introns

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25
Q

What is mRNA used for?

A

Sends a nucleotide message from the nucleus to the ribosomes

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26
Q

What is tRNA used for?

A

Transferring amino acids to polypeptides during protein synthesis

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27
Q

What is rRNA used for?

A

It forms the major components of the ribosomal subunits

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28
Q

What type of ribosomes are present in prokaryotic and eukaryotic cells?

A

Prokaryotic- 70S (50s + 30S)

Eukaryotic- 80S (60s + 40s)

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29
Q

In what direction does the coding strand run?

A

5’ to 3’

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30
Q

In what direction does the template strand run?

A

3’ to 5’

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31
Q

What does RNA polymerase do?

A

Unwinds DNA helices

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32
Q

What stops RNA polymerase

A

When it reaches a downstream termination sequence

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33
Q

What is a sequence of 3 bases known as?

A

A codon

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34
Q

How many start and stop codons are there?

A

1 start codon and 3 stop codons

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35
Q

What is the genetic code?

A

The relationship between the sequence of bases on mRNA and sequence of amino acids in a protein

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36
Q

What does degenerate mean?

A

A single amino acid may have more than one codon

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37
Q

Where does protein synthesis occur?

A

The ribosomes

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38
Q

What are ribozymes?

A

Catalytic RNA

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39
Q

How does a ribosomes form in initiation?

A

The small subunit complexes with initiation factors
Base pairing occurs between rRNA and a special sequence on mRNA
Start codon is positioned in the P site
The large subunit joins, GTP is hydrolysed and initiation factors leave the ribosome

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40
Q

How many sites within a ribosome are occupied at any one time?

A

Only two

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41
Q

What is the A site of a ribosome?

A

Aminoacyl acceptor site (point of entry)

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42
Q

What is the P site of a ribosome?

A

Peptidyl site (point of bond formation)

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43
Q

What is the E site of a ribosome?

A

The exit site

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44
Q

What is translocation?

A

Peptide chain enters the P site of the ribosome, unloaded tRNA moves to the E site, leaving the A site empty

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45
Q

How does termination occur?

A

Synthesis occurs until a stop codon is reached
A release factor binds in the A site
The polypeptide in the P site is hydrolysed from its tRNA and leaves the ribosome

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46
Q

Which antibiotics preferentially bind to prokaryotic ribosomal RNAs and proteins?

A

Tetracycline
Chloramphenicol
Erythromycin

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47
Q

Define proteomics.

A

The large scale study of proteins, in particular their structure, function and modifications

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48
Q

What is lipidation?

A

Method of localising proteins in membranes by increasing its hydrophobicity

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49
Q

What is phosphorylation? Which three residues does it principally occur on?

A

Addition of phosphate groups by kinases

Onto serine, threonine and tyrosine (OH side chain) residues

50
Q

How does glycosylation affect proteins?

A

It affects protein folding, distribution, stability and activity

51
Q

What is the purpose of acetylation on histone proteins?

A

At the amine group of lysine residues, acetylation can help to control gene expression

52
Q

What is a first order reaction?

A

When the reaction rate is not dependent on the concentration of the reactants

53
Q

What is a second order reaction?

A

Where the rate is dependent on the concentration of one reactant

54
Q

What is a third order reaction?

A

Where the rate is dependent on the concentration of two reactants

55
Q

What sign should Gibbs Free Energy have in order for the product to form?

56
Q

What is the Michaelis complex?

A

Complex formed between enzyme and substrate

57
Q

What is the Michaelis constant?

A

Km = (rate of backwards reaction + rate of production of product) / rate of forwards reaction

58
Q

What is the equation for initial rate of reaction?

A

Vo= Vmax x [So] / Km + [So]

59
Q

What is competitive inhibition?

A

Substrate and inhibitor compete for the active site

60
Q

What is uncompetitive inhibition?

A

Inhibitor binds in the active site altering its shape

61
Q

What is non competitive inhibition?

A

Inhibitor binds away from the active site, altering its shape

62
Q

What is the diameter of the nucleus?

63
Q

What percentage of the cell volume does the nucleus account for?

64
Q

What does the nuclear envelope do?

A

Encloses chromatin

65
Q

How big is a nuclear pore?

A

120nm diameter

35nm thick

66
Q

How big is an active nuclear pore?

67
Q

How big is a passive pore?

68
Q

How many pores are there in a nucleus?

69
Q

What import and export do nuclear pores allow?

A

Import of proteins with nuclear import signals- usually basic N-terminal sequence rich in lysine and arginine
Export of RNA molecules and ribosomal sub units

70
Q

What percentage of nuclear volume does fibrous chromatin occupy?

71
Q

What is nucleoplasm?

A

Amorphous fluid containing soluble components such as proteins and RNA

72
Q

What is the nucleolus?

A

Dark stained region

Where ribosomal sub units are assembled

73
Q

What is the nuclear matrix?

A

Insoluble, fibrous structure that retains the shape of the nucleus

74
Q

What is the nuclear lamina?

A

The region underneath the inner membrane

75
Q

From where to where do vesicles travel within a cell?

A

From the endoplasmic reticulum to the Golgi body

76
Q

What is the main difference between RER and SER?

A

RER- covered in ribosomes for protein synthesis

SER- more tubular for lipid and drug metabolism

77
Q

What is transitional endoplasmic reticulum?

A

Part way between RER and SER

78
Q

What organelle deals with detoxification of drugs?

79
Q

What is required for detoxification of drugs?

A

Numerous enzymes that deal with foreign substances, in order to render them harmless by oxidation, such as cytochrome P450

80
Q

What is translocation?

A

Ribosomes containing mRNA attach to the membrane of RER, and a signal recognition particle allows the translocon channel to open, causing the peptide chain to be translated and enter the lumen of the ER. Where the signal peptides enzyme removes the RNA primer from the peptide chain.

81
Q

Where does N linked glycosylation occur? And what is it?

A

It occurs in the endoplasmic reticulum and is the process of adding branched sugar chains to the N group of Asparagine residues.

82
Q

Where and how does the assembly of lipid bilayers occur?

A

In the ER, lipid synthesis only adds to the cytosolic side, specific flippase proteins catalyse the flipping of selected lipid molecules

83
Q

Which organelle is concaved and polar?

A

The Golgi body

Polarised- direction of flow

84
Q

What are the Golgi body lumen known as?

85
Q

Where does O linked glycosylation occurs? And what is it?

A

Golgi body, sugars attach to the O of the side chains of serine and threonine residues to give proteoglycans

86
Q

What name is given to a protein with a fatty acid chain attached?

A

Lipoprotein

87
Q

How are polypeptide hormones and neurotransmitters formed?

A

Synthesised in the Golgi body as inactive precursor molecules from which the active form is liberated by proteolysis using endopeptidases

88
Q

Where does protein sorting occur?

A

Trans Golgi Network

89
Q

What are the three compartments in the trans Golgi network?

A

Cis
Medial
Trans

90
Q

What is the secretory pathway in the Golgi body?

A

Lysosomes are used for intracellular digestion which contain over 40 different hydrolysis enzymes giving them a pH of 5.

91
Q

What is consecutive secretion in the Golgi body?

A

Transport vesicles designed for immediate fusion with the plasma membrane leave the Golgi in a steady stream, carrying proteins, lipids, proteoglycans etc.
The vesicles membranes also carry plasma membrane integral proteins

92
Q

What is regulated secretion in the Golgi body?

A

Receptor mediated exocytosis

93
Q

Where does polysaccharide synthesis occur?

A

The Golgi body

94
Q

What are the features of a lysosome?

A

50-500nm in diameter
High specialised membranes
Contain many acid hydrolases
PH 4.5

95
Q

What is endocytosis?

A

Receptor mediated mechanism for engulfing foreign microbes and internalising specific extra cellular molecules

96
Q

What is autophagy?

A

Selective destruction and recycling of worn out organelles by wrapping them in smooth ER membrane for digestion

97
Q

What are the four functions of lysosomes?

A

Endocytosis
Autophagy
Apoptosis
Extra cellular digestion

98
Q

What is apoptosis/autolysis?

A

Self determined destruction of a cell

99
Q

What is extra cellular digestion?

A

Lysosomal enzyme release following trauma- localised inflammation

100
Q

Define catabolic.

A

Obtaining energy by breaking down nutrients (glucose)

101
Q

Define anabolic.

A

Production of new cell components through processes that require energy, producing energy via synthesis processes

102
Q

What features do mitochondria have?

A

1 micron in diameter
Double membrane
Highly folded inner membrane
Contains 70s ribosomes

103
Q

What functions occur in the mitochondria?

A

ATP generation

Fatty acid oxidation, Krebs cycle, oxidative phosphorylation

104
Q

What are the features of a mitochondrial outer membrane?

A

Contains porin, channel forming protein

Permeable to molecules with a molecular weight below 10000

105
Q

What are the features of the inter membrane space in mitochondria?

A

Roughly equivalent to cytosol, pH 7

Many enzymes that use the ATP passing out of the matrix

106
Q

What are the features of the inner membrane of mitochondria?

A

Large surface area
75% protein
High permeable to ions

107
Q

What is the main feature of the mitochondrial matrix?

A

Alkaline pH for removal of protons

108
Q

Describe glycolysis.

A 
1x glucose -> 2x pyruvate 
Produces biosynthetically useful intermediates such as folic
Occurs in cytosol
Net production of 2x ATP
Coenzyme production is 2x NADH
109
Q

How are lipids metabolised?

A

Lipids are stored as triglycerides and when broken down the glycerol can be used in glycolysis.
Fatty acyl coA chains are broken down using a coA enzyme to produce acetyl coA and another (shorter) fatty acyl coA chains beta oxidation.

110
Q

What is oxidative phosphorylation?

A

Occurs in the inner membrane of mitochondria. An NADH Hydrogenase molecule in the membrane removes protons and electrons from the NADH molecules produced. Protons travel down a concentration gradient through an ATP Synthase molecule in the membrane. The enzyme spins, releasing ATP.

111
Q

Where are actin filaments in a cell and what do they do?

A

Anchored just below the plasma membrane and are responsible for changing the shape of the cell by contracting or relaxing

112
Q

What are microtubules responsible for?

A

Movement of organelles and vesicles

113
Q

What are the three types of motor protein?

A

Myosins
Kinesins
Dyneins

114
Q

What is the diameter of a microtubule?

115
Q

What is tubulin?

A

A dimer made up of alpha and beta units that forms microtubules

116
Q

How does a microtubule form?

A

Protofilaments are arranged in a tube with a hollow core, they stick together at an angle of 160 degrees allowing it to curve into a tube.

117
Q

What are axonemal microtubule structures?

A

Complex structures formed from microtubule bundles such as flagella

118
Q

What are the differences between cilia and flagella?

A 
Cilia- 5-10um length
Present in large numbers
Complex biphasic movement
Flagella- up to 150um length
Few in number
Wave of motion propels cell
119
Q

What is the diameter of an action filament?

120
Q

What are the features of an action filament?

A

One end is often attached to the plasma membrane
Solid filaments extend throughout the cell
Important in whole cell movement

121
Q

What is the diameter of an intermediate filament?

122
Q

What are the features of intermediate filaments?

A

Found only in animal cells
Size varies depending on the protein
Composed of fibrous proteins
Structural/tension bearing role

Pharm Y1 (11 decks)

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