TBL 1 Cells and Organelles Flashcards

1
Q

Eukaryotic cell size is limited by a minimum and maximum.

The lower limit is __________; whereas the upper limit is __________.

A

Lower limit: Least cell volume required to fit all organelles

Upper limit: Maximum volume such that the surface area-to-volume ratio for exchange of substances is not compromised.

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2
Q

The cell ________ (organelle) is responsible for the control of cellular organisation and all cellular activities.

A

nucleus

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3
Q

The nucleus is embedded with specialised pore complexes, _________, allowing for the movement of resources to and from the nucleus.

A

Nuclear pores

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4
Q

The nucleus has a DOUBLE membrane (__________) that becomes continuous with the __________(organelle), allowing for continuous passage of mRNA to ribosomes embedded in the membrane of the ER.

A

nuclear envelope; rough ER

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5
Q

Endosymbiotic theory: _________ and ________ (organelles in eukaryotes) are believed to be derived from the incorporation of prokaryotic cells.
Both of them have their own _______ DNA.

A

mitochondria and chloroplast; circular DNA

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6
Q

Conventional light microscopes allow us to see up to ___ (units); whereas electron microscope allows us to see up to ___.

A

Light - micrometres

Electron - nanometres

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7
Q

________ motion is the spontaneous movement of molecules into and out of the cells, and is what allows molecules to diffuse freely.

A

Brownian motion

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8
Q

__________ converts angiotensin I to bioactive angiotensin II which helps to (increase/decrease) blood pressure.

A

Angiotensin Converting Enzyme (ACE)

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9
Q

___________ is responsible for the removal of phosphate from glucose-6-phosphate to increase the bioavailability of glucose. It cleaves phosphate to allow the release of glucose into the bloodstream when the blood glucose level is low.

A

Glucose-6-phosphatase

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10
Q

__________ (Clinical condition) is an autosomal recessive disorder resulting from G6PD deficiency. (low levels of glucose-6-phosphatase enzyme –> hypoglycaemia)

A

Von Glerke’s disease

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11
Q

Enzymes act by _________ that impede chemical reactions from happening.

A

lowering activation energy

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12
Q

The first law of thermodynamics states that

A

Energy can neither be created nor destroyed. (only converted)

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13
Q

The second law of thermodynamics states that

A

Any isolated system tends towards entropy/disorderliness. (i.e. degree of disorder can only increase)

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14
Q

Biological systems are very well-ordered - they follow the second law of thermodynamics by taking energy from the _________ surrounding the cell and investing it in chemical reactions which maintain order.

A

take energy from surrounding environment

=> increased disorder as a whole system

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15
Q

________ is the amount of energy within the molecule that can perform useful work at a constant temperature.

A

Gibbs free energy

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16
Q

delta(G) =

A

free energy of products - free energy of reactants

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17
Q

Change in Gibbs free energy is a measure of the change in order within the cell and change in entropy of the system.

A

-

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18
Q

Reactions are spontaneous if delta(G) <0 (exergonic) or >0 (endogenic)?

A

delta(G) < 0

i.e. free energy of reactants > free energy of products

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19
Q

Do enzymes change the delta(G) of the reaction?

A

No. Spontaneous reactions (i.e. delta(G) <0) might not proceed due to slow kinetics, so enzymes are used to speed up the rate without changing delta(G) of the reaction.

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20
Q

Anabolic reactions are generally energetically unfavourable (i.e. delta(G) <0), so how do cells overcome this problem?

A

Couple anabolic reactions to energetically favourable reactions like ATP hydrolysis –> delta(G overall) > 0 and is therefore spontaneous.

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21
Q

In ATP hydrolysis, energy is released through the hydrolysis of __________ bonds.

A

Phosphoanhydride bonds

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22
Q

__________ is the minimum amount of energy that reactants need to possess before the reaction can proceed.

A

Activation energy

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23
Q

Catalytic amino acid residues within the enzyme participate in the creation/breaking of bonds of substrates by ______________.

A

altering electron arrangement (redox reactions)

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24
Q

Stressing bonds i.e. ________ of substrate molecules into a certain shape causes them to resemble the _________, which is a particular conformation where atoms are rearranged geometrically and electrically so they are more susceptible to reaction.

A

Contortion; transition state

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25
Q

The _________ hypothesis states that the 3D conformation of the substrate is completely and exactly complementary to that of the enzymatic active site.

A

lock-and-key

=> only bind to one substrate and catalyse one reaction (Substrate specificity)

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26
Q

The ________ hypothesis suggests that the 3D conformation of the substrate is not completely complementary to that of the enzymatic active site.

A

induced fit
=> accounts for the ability of enzymes to bind to substrates which are structurally/chemically similar
(group specificity)

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27
Q

_______ is a component of tears and nasal secretions and serves as a first line of defence against bacterial infections.

A

Lysozyme

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28
Q

Lysozyme functions to catalyse ________.

A

catalyse the hydrolysis of sugar molecules within the bacterial cell walls (cells are induced to undergo lysis and die).

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29
Q

Substrate of lysozyme:

A

Alternating polysaccharide co-polymers of N-acetyl glucosamine (NAG) and N-acetyl muramic acid (NAM) - unit structure of bacterial cell walls.

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30
Q

Lysozyme cleaves at the __________ connecting C_ of NAM to C_ of NAG.

A

cleaves at the B(1,4) glycosidic linkage connecting C1 of NAM to C4 of NAG

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31
Q

Lysozyme (protein enzyme) secondary structure:

A

both alpha helical and B pleated sheets

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32
Q

Lysozyme (acidic/basic) catalytic amino acid residues:

A

Glutamate-35 and Aspartic acid-52

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33
Q

Structure and function of lysozyme:

_____ (AA) protonates oxygen in the glycosidic bond, breaking the bond holding the sugar molecules together.

Water molecule enters and is deprotonated by _____.

_____ (AA) stabilises the positive charge in the transition state, while the OH- ion attacks the ____ carbocation to add a -OH group.

A

Glu-35 protonates oxygen, breaking bond.

Glu-35 accepts H+ from H2O, forming OH-.

Asp-52 stabilises positive charge, while -OH ion attacks the NAM carbocation to add a OH group.

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34
Q

The optimum pH for lysozyme enzyme is ___, when Glu-35 is (unionised/ionised) and Asp-52 is (unionised/ionised).

A

pH 5.0

Glu-35 is unionised; Asp-52 is ionised

35
Q

Proteins are a group of organic compounds that is composed of ___% of our human body.

A

20%

36
Q

Amino acids with positively-charged R groups are (acidic/basic).

A

Basic (i.e. can accept H+)

37
Q

Amino acids with negatively-charged R groups are (acidic/basic).

e.g. Asp and Glu (lysozyme)

A

Acidic (i.e. can donate H+ to form negative charge)

38
Q

______ (AA) has a 5-membered ring involving backbone N atom, causing steric hindrance in the backbone –> kinks.

A

Proline

39
Q

Amino acids can act as buffers (resist small changes to pH) by forming _________.

A

zwitterions

40
Q

______ is the only amino acid that is non-chiral.

A

Glycine

41
Q

All natural endogenous amino acids are of the ___-form.

A

Laevorotary (L)-form: i.e. rotates plane polarised light to the left.

42
Q

Polypeptide chains are formed from the _______ of amino acids. A covalent peptide bond is formed between __________.

A

condensation of amino acids

covalent peptide bond formed between the amine group of one amino acid and the carboxyl group of the other amino acid

43
Q

Proteins will assume a conformation where the folding is of ________ energy, by maximising _______ and _________ bonds.

A

lowest energy; maximising hydrogen and covalent bonds

44
Q

_______ bind to partially folded polypeptide chains to ensure that folding continues along the most energetically feasible pathway.

A

Chaperones

45
Q

Why are C=O and N-H bonds of each peptide always on the same plane?

A

Because the C=O bonds on amino acids restrict free rotation

46
Q

Proteins can be denatured using _____ to break the H bonds in the secondary, tertiary and quaternary structures.

A

urea

47
Q

Proteins can be denatured using 2-mercaptoethanol, which breaks _______ bonds.

A

disulphide bonds

48
Q

a-helices have hydrogen bonds formed between amino acid residues ___ positions apart. One turn spans ___ amino acid residues, with side chains projecting outwards.

A

bind to amino acid residues 4 positions away

each span 3.6 AA residues

49
Q

Amino acids a-helices are ____-handed.

A

right-handed a-helices (due to L-form AA)

50
Q

Proline residues terminate the a-helix due to:

A

large 5-membered ring structure that restricts the C-N bond rotation and prevents hydrogen bond formation —> kink is inserted and helix is terminated.

51
Q

Disulfide bonds are formed from the _______ of ______ side chains.

A

oxidation of 2 cysteine amino acid side chains

52
Q

Many blood clotting factors contain N-terminal glutamate residues that must be modified by __________ via a carboxylation reaction to form ________ which enhances the calcium-binding capabilities of the factor.

A

N-terminal glutamate residues to be modified by vitamin K-dependent carboxylase to form y-carboxyglutamate

53
Q

For vitamin K to be functional (for vitamin K-dependent carboxylase to work and produce suitable blood clotting factors), it must be reduced by __________.

A

vitamin K epoxide reductase

54
Q

_______ is an anti-coagulant drug which prevents blood from clotting.

A

Warfarin

55
Q

What is the main mechanism of action of Warfarin?

A

It inhibits vitamin K epoxide reductase, thereby reducing the levels of functional Vitamin K, impairing the function of vitamin K-dependent carboxylase. The enzyme therefore cannot carboxylate glutamate to form y-carboxyglutamate, reducing calcium-binding capability and reduced blood clotting.

56
Q

Phospholipids are ______ (contain both hydrophilic and hydrophobic groups).

A

amphiphilic

57
Q

All phospholipids contain __________.

A

1 glycerol connected to 2 fatty acid chains and 1 phosphate group

58
Q

Saturated fatty acid chains are (less/more) densely packed.

A

more densely packed (membrane less fluid)

59
Q

Phosphatidylcholine (also known as _______) is a common phospholipid in the membrane bilayer. It is found as a lung surfactant to reduce surface tension of small alveoli.

A

lecithin

60
Q

_________ is a membrane constituent which regulates membrane fluidity and permeability depending on the temperature and nature of the membrane.

A

Cholesterol

61
Q

The short hydrophobic tail of cholesterol functions to __________.

A

anchor the cholesterol to the lipid bilayer

62
Q

The planar steroid ring of cholesterol causes __________.

A

stiffening of the cell membrane

63
Q

The polar head of cholesterol functions to ________.

A

anchor cholesterol to the lipid bilayer via hydrogen bonds with the phospholipid heads.

64
Q

At low temperatures, cholesterol will (increase/decrease) membrane fluidity by _________.

A

Increase membrane fluidity by preventing the phospholipids from packing too closely by intercalating between them.

65
Q

At high temperatures, cholesterol (increases/decreases) membrane fluidity by ___________.

A

Cholesterol decreases membrane fluidity at high temperatures by forming hydrophobic interactions with the hydrophobic tails of the phospholipids –> interfering with chain flexing and lateral diffusion

66
Q

Cholesterol (reduces/increases) membrane permeability.

A

Reduces membrane permeability.

It plugs transient pores between phospholipids.

67
Q

Membranes are asymmetrical in nature.

A
  • Glycolipids are on the extracellular side of membrane.

- Negative charges are inside the cell.

68
Q

________ of phospholipids is when lipids diffuse within the monolayer (i.e. swap places).

A

Lateral diffusion (frequent)

69
Q

_______ is the process of lipids switching sides in the bilayer.

A

Flip-flop (rare)

70
Q

The fluid mosaic model suggests that:

A

the presence of integral proteins (unilateral/transmembrane) or peripheral proteins which will increase membrane fluidity as it breaks the orderly fashion of the membrane

71
Q

Fence & Picket model:
Membrane proteins were found to be constrained in their movement.
Proteins were constrained by fences (__________).

A

Membrane cytoskeleton

=> Actin filaments on cytosolic side of membrane form spaces where proteins can move freely.

72
Q

DNA is (more/less) stable then RNA due to the ________.

A

DNA is more stable than RNA due to the lack of -OH group on C2. (less reactive, and allows for closer packing of molecule)

73
Q

Purines include ______ and ______. They have a __-ringed structure.

A

Guanine and Adenine; 2-ringed structure

74
Q

Pyrimidines include ______, ______ and _____. They have a __-ringed structure.

A

Cytosine, Uracil and Thymine; 1-ringed structure

75
Q

Nucleosides are nucleotides without _______.

A

Without phosphate groups

i.e. sugar + base

76
Q

Up to ___ phosphate groups can be linked to the __’ carbon of the sugar via ________ bonds to form nucleotides.

A

Up to 3 phosphate groups; linked to C5 of sugar via phosphoester bonds.

77
Q

DNA and RNA sequences are read from the __’ to __’ direction

A

5’ to 3’

78
Q

DNA is a (right/left-) handed double helical structure with antiparallel strands running in opposite directions.

A

right-handed helical structure

79
Q

2 DNA strands (to form a single double helix) are held by 2 types of forces:

A
  1. Hydrogen bonds between the bases

2. Hydrophobic interactions between adjacent base-pairs (stacking)

80
Q

__ hydrogen bonds between Adenine and _____.

__ hydrogen bonds between Cytosine and ________.

A

2 H bonds: A and T/U

3 H bonds:
C and G

81
Q

To denature DNA, use high temperature or _________.

A

low salt concentration

82
Q

To reanneal DNA, use low temperature or __________.

A

high salt concentration

83
Q

During interphase, DNA exists as chromatin which has 2 forms:
________ (loosely condensed)

___________ (highly condensed)

A

Euchromatin (loosely condensed –> Transcriptionally active)

Heterochromatin (highly condensed —> Transcriptionally inactive)