Lipids & Proteins Flashcards

1
Q

Examples of macromolecules

A

Triglycerides, phospholipids

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2
Q

Structure of a triglyceride

A

Three fatty acids bonded to one glycerol by ester bonds which form through condensation reactions

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3
Q

How do ester bonds form in triglycerides?

A

Hydroxyl groups on glycerol and fatty acids interact with each other, form three water molecules (One for each fatty acid)

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4
Q

Name of the process of triglycerides forming

A

Esterification

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5
Q

Structure of fatty acids

A

A carboxyl group with a hydrocarbon chain attached

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6
Q

What does it mean if a fatty acid is saturated?

A
  • carbon atoms have maximum number of hydrogen atoms bonded to them.
  • NO double bonds
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7
Q

Monounsaturated

A

One double bond

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8
Q

What do double bonds in fatty acids cause?

A

Kinks and bends

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9
Q

Effect of kinks and bends in a fatty acid

A

They can’t pack so closely together.

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10
Q

How do triglycerides form?

A

Ester bonds form when the hydroxyl groups of the glycerol and the fatty acids interact, three water molecules form

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11
Q

How do you break down triglycerides?

A

Three water molecules are supplied which reverse esterification in a hydrolysis reaction.

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12
Q

Structure of phospholipids

A

Non-polar and hydrophobic tail (The fatty acids), charged and hydrophilic head (Phosphate group)

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13
Q

How the properties of phospholipids relate to their purpose?

A

Act as surfactants
* hydrophilic head will be in water
* hydrophobic fatty acid tails won’t, in

  • phospholipid bilayers the hydrophobic tails point towards the centre of the sheet
  • bilayer allows it to form cell membranes in aqueous environments
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14
Q

Functions of phospholipids

A

Surfactants, phospholipid bilayers in cell membranes

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15
Q

What is cholesterol?

A

Sterol

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16
Q

Structure of cholesterol

A

Hydrophobic four carbon ring, hydrophilic hydroxyl groups

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17
Q

How do the properties of cholesterol link to its function?

A

Hydrophilic hydroxyl group at the periphery of a membrane regulates the fluidity

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18
Q

Functions of lipids

A

Membrane formation, hormone production, electrical insulation, waterproofing, thermal insulation, cushioning of vital organs, buoyancy

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19
Q

Example of lipids being used in waterproofing

A

Bird feathers, plant leaves

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20
Q

Example of lipids being used in thermal insulation

A

Penguins

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21
Q

Example of lipids being used in buoyancy

A

Whales

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22
Q

How do dipeptides form?

A
  • Hydroxyl in the carboxylic acid group of one amino acid reacts with hydrogen in an amine group of another amino acid
  • peptide bond forms
  • water released (condensation reaction)
23
Q

How do polypeptides form?

A
  • Amino acids joined together by peptide bonds
  • catalysed by peptidyl transferase in ribosomes,
  • different R groups interact with each other to form different kinds of bonds
24
Q

What are the levels of protein structure?

A

Primary, secondary, tertiary, quaternary

25
What is the primary structure of a protein?
* sequence of amino acids in the polypeptide * influences how the protein will fold * Only peptide bonds are involved
26
What is the secondary structure of a protein?
* interaction of the oxygen, nitrogen and hydrogen atoms of the amino acids * in the carboxylic acid group and the amine group.
27
Secondary structure
* interaction of H, O, N atoms of amino acids * in carboxylic group and amine group * structure: a-helix and b-pleated sheets
28
How do alpha helices form?
Hydrogen bonds form within the chain, pulling it into a coil shape.
29
How do beta pleated sheets form?
* polypeptide chains lie parallel to each other * join by hydrogen bonds * pattern formed by amino acids causes structure to look pleated.
30
What causes secondary structure?
Hydrogen bonding which depends on the amino sequences of the long protein molecules
31
What is the tertiary structure of a protein?
* Folding of a protein into its final shape * caused by coiling and folding into the secondary structure
32
Examples of interactions that can occur between amino acid R groups
Hydrophobic/Hydrophilic Interactions, hydrogen bonds, ionic bonds, disulphide bonds
33
Cause of hydrophobic/hydrophilic interactions between amino acid R groups
Interactions between polar and non-polar R groups
34
Cause of ionic bonds between amino acid R groups
Oppositely charged R groups
35
Cause of disulphide bonds between amino acid R groups
Covalent bonds form between R groups of amino acid that contain sulfur atoms.
36
Examples of globular proteins
Haemoglobin, catalase, insulin
37
General structure of globular protein
Compact, water soluble, roughly spherical, hydrophobic R-groups on the amino acids are kept away from the aqueous environment, hydrophilic R-groups on the outside of the protein
38
Structure of insulin
Made up of two polypeptide chains that are linked together by disulphide bonds. Both chains are alpha helices.
39
Structure of catalase
Quarternary protein with four haem prosthetic groups.
40
Structure of haemoglobin
Quarternary protein made up of two alpha polypeptides and two beta polypeptides, each of which has a haem group containing an Fe^2+ ion.
41
Function of insulin
To regulate blood glucose concentration.
42
Conjugated proteins
Globular proteins with a prosthetic group
43
Prosthetic groups
Non-protein attachments to a globular protein
44
Function of haemoglobin
To transport oxygen around the body
45
Function of catalase
To speed up the breakdown of hydrogen peroxide
46
Examples of fibrous proteins
Collagen, keratin, elastin
47
General structure of fibrous proteins
Long, insoluble molecules, high proportion of amino acids with hydrophobic R groups, limited range of amino acids, repetitive primary structure leading to organised structures
48
Properties of keratin
Strong, inflexible, insoluble
49
Function of keratin
To form hair, skin and nails, to help epithelial cells maintain integrity.
50
Properties of collagen
Flexible, strong
51
Function of collagen
To be a connective tissue in skin, tendons, ligaments and the nervous system.
52
Properties of elastin
High resilience for large strains, low stiffness, flexible
53
Function of elastin
To give structures like the walls of blood vessels and the lining of the lungs the flexibility to expand when needed.