Topic 1 - Module 4 Flashcards

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1
Q

Describe 3 broad areas for lipid functions and provide examples.

A
  1. Storage, such as fatty acids, triacylglycerols, and waxes.
  2. Structural lipids, such as phospholipids, glycolipids, cholesterol, sphingolipids, and glycerolphospholipids.
  3. Signaling and cofactor lipids, such as phospholipid derivates, steroid hormones, lipid-soluble vitamins and eicosanoids.
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2
Q

Define “lipids” and distinguish them from other biological molecules.

A

They are generally non-polar and have low solubility in water, and high solubility in organic solvents.
Predominantly used for energy storage, structural components and to a lesser extent, in signalling and as cofactors.

Proteins are more abundant as signaling and receptor molecules, compared to lipids.

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3
Q

What formation does the addition of free fatty acid molecules to an aqueous solution at physiological temperatures tend to favour and why?

A

Formation of micelles.

The hydrophobic regions are buried deeply in the core, and tightly packed fatty acid tails will exclude water from the region - increasing entropic gain due to release of ‘ordered’ water, thermodynamically stabilising the structure.

As a bilayer, the hydrophobic edges are exposed to aqueous solution, making it energetically unstable.

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4
Q

What is the difference between phospholipids and fatty acids?

A

Fatty acids are wedge-shaped units (cross-section of phosphate head is greater than their single side chain) that will form micelles when packed together.

Phospholipids are individual units that are cylindrical units (phosphate head = side chains (2)) and forms lipid bilayers.

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5
Q

For a fully saturated fatty acid chain, describe its physical and chemical properties.

A

As the length of the hydrocarbon chain increases, the melting point increases, alongside decrease in water solubility.

This is because its composition enables it to tightly pack into a crystalline array (liquid) while stabilised by extensive interactions with the acyl chain with one another.
Release of ordered water will lead to an increase in entropic gain, via condensation reactions, leading to the spontaneity of reactions.

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6
Q

Explain the physical properties of unsaturated fatty acids by describing the natural conformation.

A

Generally, the unsaturated fatty acids will have their double bonds in cis formation, as the biosynthetic pathway via enzymes are unable to produce “trans” isomers.
This then creates less favourable steric interactions, and hence, will require less thermal energy to disrupt the disordered packing of the acids - resulting in lower melting point.

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7
Q

Differentiate trans fatty acids from typically unsaturated cis fatty acids.

A

Trans fatty acids are formed by the partial dehydrogenation of unsaturated fatty acids in food processing. The trans double bond enables the molecule to pack more regularly, resulting in a higher melting point than their cis counterparts.

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8
Q

Define triacylglycerols and then describe the different types of triacylglycerols.

A

They are fatty acid esters of glycerol, involving one glycerol molecule bonded to 3 fatty acid chains.

  1. simple triacylglycerols have the same, identical fatty chains.
  2. mixed triacylglycerols have different fatty acids
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9
Q

Describe the properties of triacylglycerols

A

They provide stored energy and insulation, and are generally uncharged, hydrophobic molecules.

advantages include higher energy yield per molecule (compared to oxidation of other sources such as glycogen or starch) due to their hydrophobic nature - making them lighter - while expending less energy on releasing water.

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10
Q

Explain the functional significance of membrane lipids and their formation.

A

They are generally a lipid bilayer with a hydrophobic core, this means that they are also a barrier to the movement of hydrophilic molecules into the cell.

They are formed via spontaneous reaction whereby the burial of the hydrophobic core leads to entropic gain as order water is being released.

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11
Q

Differentiate the two types of phospholipids, which both have distinctive signalling roles.

A
  1. glycerolphospholipids have an alcohol group attached to the phosphate group
    - the charge is individually determined, and dependent on identity of the substituent alcohol group.
  2. sphingolipids have a choline group attached to their phosphate group, and sphingosine backbone (derived from amino alcohol sphingosine)
    - contains amide linkage, instead of ester linkage
    - will contribute to 1 out of the 3 tails (like glycerol)
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12
Q

Which type of membrane lipid is used in the outer membrane leaflet and as determinants of the blood groups (ABO) - then explain why.

A

Glycolipids are components of the outer membrane leaflets as it can contribute to sites of biological recognition (as a signalling molecule) while also as part of glycosphingolipids to be determinants of antigens.

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13
Q

Describe the chemical structural properties of sterols

A

They have 4 fused carbon rings, which constrains their conformation, making them almost planar and relatively rigid.

Predominantly hydrophobic, enabling it to interact with various other non-polar groups, such as lipids. But they are amphipathic molecules due to polar -OH group.

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14
Q

Explain the role of cholesterol as a signalling molecule.

A

In addition to its structural role in membranes, cholesterol can act as a precursor for the synthesis of steroid hormones.

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15
Q

Summarise the membrane composition and properties, in terms of the fluid mosaic model.

A

Proteins embedded in the bilayer are held by hydrophobic interactions, which is what allows fluid dynamic properties.

Charges of the lipid head groups contribute significantly to surface properties of the membrane, as it allows recognition of membrane components.

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16
Q

Define the phase transition temperature and explain it in terms of membrane fluidity.

A

The temperature at which the membrane goes from paracrystalline into a fluid state.

Increasing temperature will mean that membrane fluidity increases as acyl chains have become fluid, while the lipid itself can laterally diffuse into another position within the bilayer.

At 37 degrees, all biological membranes are fluid.

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17
Q

Explain the difference between lateral and transverse lipid diffusion.

A

Uncatalyzed lateral diffusion occurs rapidly, whereas transverse “flip-flop” diffusion occurs very slowly.
This is because the polar head group needs to travel or be pushed through nonpolar acyl chains, a movement that is highly energetically unfavorable.

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18
Q

How is transverse “flip-flop” diffusion facilitated?

A

Through the process of catalysis, such as the use of specialised proteins embedded in the bilayer, the trans-bilayer movement can be made energetically more favourable and faster than uncatalyzed lateral diffusion.

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19
Q

What is the Fluorescence recovery after photobleaching (FRAP) technique useful for?

A

The FRAP technique measures the rate of fluorescence return over a given area of phospholipids, which determines the rate of lipid diffusion across the membrane.

20
Q

Define ‘sidedness’ in terms of the bilayer membrane and explain its significance.

A

A ‘sidedness’ is a difference in lipid composition on either side of the bilayer.
Catalysis involves moving down a concentration gradient, hence sidedness of lipid composition will inherently facilitate catalysis and movement of substances across the membrane.

By detecting this difference in composition, you can easily identify potential cell death when inner monolayer components are showing an increasing concentration.

21
Q

What are membrane rafts made of? Explain the functional significance of these membrane rafts.

A

They are mostly made of clustered sterol and sphingolipids, with different localized proteins (would form transient interactions with lipids) that promotes efficient signalling both in and out of the cell.

22
Q

Compare the properties of peripheral and integral membrane proteins

A

Peripheral proteins are typically attached to integral membrane proteins, through ionic interactions and H-bonding, while associating with outside surfaces.

Integral membrane proteins themselves are firmly attached to the membrane, usually embedded within it. They have extensive hydrophobic interactions with AA residues at the surface of membranes, and also with the acyl chains of lipids within the membranes.

23
Q

Describe how peripheral membrane proteins can be experimentally released from biological membranes.

A

Peripheral proteins are released from membrane by reagents that disrupt the ionic interactions formed with integral proteins, such as high salt concentrations (disrupts salt bridges), changes in pH (changes charged state of groups in salt bridges) and chelating agents that can add/remove metal that forms base of salt-bridge interactions.

24
Q

Explain the differences and similarities between active and passive transport across a biological membrane

A

The major distinction between passive and active transport is still whether it is against the concentration gradient, and whether the transport requires energy (i.e. ATP).

Passive transporters are known to be able to undergo conformational changes during the transport process and participate in facilitated diffusion of specific molecules.

Active transporters will also undergo conformational changes that isn’t solely driven by hydrolysis of ATP to ADP, phosphorylation stabilizes this conformational changes.

25
Q

Provide an example of an active transporter and a passive transporter, describing their mechanism of action.

A

GLUT1 is a passive transporter that has two conformational changes (T1 and T2) that enables it to transport glucose through the lipid bilayer. A high [glucose] in blood plasma will enable T1 state to bind glucose, upon binding, initiates a conformational change, using thermal energy, to T2, where glucose is released in the cell.

An active transporter would be the P-type ATPases that use ATP hydrolysis reactions to pump ions across the membrane. This is because the hydrolysis of ATP to ADP is energetically more stable, inducing a continuous cycle of conformational changes to drive consecutive reactions, ending with phosphorylation to stabilize the conformational changes.

26
Q

Explain the significance of the hydropathy index, and provide an example.

A

The hydropathy index is a measure of the polarity of each amino acid sequence, derived from the free energy changes needed to move the sequence from an organic solvent to water.
Hydrophobic residues will find the move unfavorable, so the reaction will be non-spontaneous, and result in a positive hydropathy index value. These residues will be embedded within the transmembrane region.

27
Q

Describe the difference between artificial and normal lipid bilayers.

A

artificial bilayers are impermeable to most water-soluble molecules because they lack the protein channels needed to process those molecules, given that transport proteins are specific to transferring particular types of molecules.

28
Q

Describe the difference between artificial and normal lipid bilayers.

A

artificial bilayers are impermeable to most water-soluble molecules because they lack the protein channels needed to process those molecules, given that transport proteins are specific to transferring particular types of molecules.

29
Q

Referring to the structure of glucose transporters, explain the significance of the positioning of its hydrophobic and polar regions.

A

The transporter (collectively made of transmembrane alpha-helices) needs to interact with both lipid side chains and polar molecules. Therefore, the hydrophobic residues are on the outside of the helical structure, with a polar, hydrophilic channel formed down the centre. The interface created will enable glucose to easily pass through the channel as the result, whereby the changing conformations are powered by thermal energy alone.

30
Q

List the 3 different roles of sugars in biology

A

They can act as information molecules (information about structural diversity), with cell surface sugars as signalling molecules, and as structural components (cellulose, chitin)

31
Q

Provide examples of different roles of carbohydrates in biology

A

Glucose units are generally used as structural units, in cellulose and chitin.

Oligosaccharides are used in ABO antigens, an example of cell-to-cell signalling

Cell surface molecules can also enable viral attachment to host cells

32
Q

Explain the difference between aldose and ketose sugars

A

Aldoses involve an aldehyde group (CH=O), whereas ketoses will have a ketone group (C=O)

Aldoses have the potential to be chiral molecules, where they form enantiomers of one another (D and L sugars) and their D-forms are naturally occurring sugars.

33
Q

Explain the structural basis of the interconversion between the alpha and beta anomers of cyclized sugars

A

Open chain hexoses cyclize into pyranose rings, and aldohexoses will have C1 aldehyde react with C5 hydroxyl group to form an intramolecular hemiacetal.

As the aldehyde group can have the oxygen atom point upwards or downwards, it will form beta and alpha anomers respectively.

34
Q

Identify the difference between reducing and non-reducing sugars in oligosaccharides

A

The non-reducing end doesn’t have the anomeric carbon exposed, whereas the reducing end does have an anomeric carbon exposed.

On the reducing sugar, the aldehyde group is free to act as a reducing agent.

35
Q

Explain how the linkages between glucose units in cellulose give rise to their structural properties.

A

The difference between reducing and non-reducing sugars means that glucose units can be linked with directionality.
Cellulose are unbranched homopolysaccharides, long linear chains that can pack tightly, and are linked via beta - 1,4 - glycosidic linkages.

36
Q

Explain how the linkages between glucose units in glycogen give rise to their different properties.

A

The difference between reducing and non-reducing sugars means that glucose units can be linked with directionality.
Glycogen are branched homopolysaccharides, branch points are connected to the main chain by alpha - 1, 6 - linkage. But the main chain is also linked by alpha - 1, 4 - linkages.
They show an open helix structure and isn’t linear, making it optimized to store sugar and render it highly accessible.

37
Q

Explain the structural difference between cellulose and chitin

A

Chitin is a linear homopolymer of N-acetylglucosamine residues and is a modified version of cellulose, where the N-acetyl group is added at C2.

38
Q

List the amino acids that can act as glycosylation sites on proteins

A

There are two options: amide link or a hydroxyl link.

Asparagine and Serine/Threonine

39
Q

Differentiate between N-linked and O-linked protein glycosylation

A

N - glycans involve asparagine being linked to the oligosaccharides via their amide side chains. O - glycans involve Serine/Threonine being linked via the hydroxyl groups.

For oligosaccharide assembly, the monosaccharide is transferred from the nucleotide sugars to the non-reducing end of the carbohydrate acceptor.

40
Q

Describe the role and general reaction of glycosyltransferase

A

In protein glycosylation, glycosyltransferase has specificity for the sugar and will always link the particular target/prime sugar in that specific way.

Hydrolyzes the nucleotide-monosaccharide bond, and transfers the monosaccharide from the nucleotide sugar to the non-reducing end of the carbohydrate acceptor.

Resulting in the nucleotide being released at end.

41
Q

Describe the structural difference between ABO blood group antigens

A

O antigens are the base carbohydrate molecule; A and B antigens have an additional monosaccharide that result from their alleles that encode active enzymes (glycosyltransferase)

42
Q

Explain ABO blood group incompatibility

A

ABO blood group incompatibility is due to the individual having antibodies against the antigens of other blood groups. However, O antigens have naturally occuring A and B antibodies, and will show incompatibility against all other blood types, resulting in hemolysis.

43
Q

Describe, with an example, the interaction between a C-type lectin and a carbohydrate

A

C-type lectins are a type of protein that recognizes specific carbohydrates, each with different carbohydrate-binding specificity.
Type C lectins are known for their calcium binding abilities, and will form an octahedral complex around calcium, partially with the sugars.

44
Q

Explain how the antiviral drug Relenza interferes with the influenza life cycle

A

Relenza is an analogue of sialic acid and will inhibit neuraminidase from binding to influenza particles, which prevents virion/viral DNA from being released. This will slow down the progression of the infection, stopping the propagation of the virus, resulting in milder effects of the flu.

45
Q

Explain what changes the binding specificity of the lectin.

A

A change in residues that are binding with the sugars will alter the binding specificity of the lectin, due to the specific OH interactions (and arrangements) needed to bind to the right sugars.

46
Q

Describe the mechanism of selectins

A

Selectins operate based on cell-to-cell adhesion and will bind to WBC at the sites of injury and guide the movements of immune system cells from the bloodstream into the infected cell. They will also increase in number around the injured site, to localize immune cells more effectively.
As such, the speed of leukocytes approaching the infected site will decrease when interacting with p-selectins.

47
Q

Explain what lectins are and their functional significance.

A

Lectins are a broad family of proteins that recognize carbohydrates; exemplifies how carbohydrates are used as signalling molecules.