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Biology: Module 2: Foundations in Biology > Lipids & Proteins > Flashcards

Lipids & Proteins Flashcards

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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
Q

What is the primary structure of a protein?

A
  • sequence of amino acids in the polypeptide
  • influences how the protein will fold
  • Only peptide bonds are involved
26
Q

What is the secondary structure of a protein?

A
  • interaction of the oxygen, nitrogen and hydrogen atoms of the amino acids
  • in the carboxylic acid group and the amine group.
27
Q

Secondary structure

A
  • interaction of H, O, N atoms of amino acids
  • in carboxylic group and amine group
  • structure: a-helix and b-pleated sheets
28
Q

How do alpha helices form?

A

Hydrogen bonds form within the chain, pulling it into a coil shape.

29
Q

How do beta pleated sheets form?

A
  • polypeptide chains lie parallel to each other
  • join by hydrogen bonds
  • pattern formed by amino acids causes structure to look pleated.
30
Q

What causes secondary structure?

A

Hydrogen bonding which depends on the amino sequences of the long protein molecules

31
Q

What is the tertiary structure of a protein?

A
  • Folding of a protein into its final shape
  • caused by coiling and folding into the secondary structure
32
Q

Examples of interactions that can occur between amino acid R groups

A

Hydrophobic/Hydrophilic Interactions, hydrogen bonds, ionic bonds, disulphide bonds

33
Q

Cause of hydrophobic/hydrophilic interactions between amino acid R groups

A

Interactions between polar and non-polar R groups

34
Q

Cause of ionic bonds between amino acid R groups

A

Oppositely charged R groups

35
Q

Cause of disulphide bonds between amino acid R groups

A

Covalent bonds form between R groups of amino acid that contain sulfur atoms.

36
Q

Examples of globular proteins

A

Haemoglobin, catalase, insulin

37
Q

General structure of globular protein

A

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
Q

Structure of insulin

A

Made up of two polypeptide chains that are linked together by disulphide bonds. Both chains are alpha helices.

39
Q

Structure of catalase

A

Quarternary protein with four haem prosthetic groups.

40
Q

Structure of haemoglobin

A

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
Q

Function of insulin

A

To regulate blood glucose concentration.

42
Q

Conjugated proteins

A

Globular proteins with a prosthetic group

43
Q

Prosthetic groups

A

Non-protein attachments to a globular protein

44
Q

Function of haemoglobin

A

To transport oxygen around the body

45
Q

Function of catalase

A

To speed up the breakdown of hydrogen peroxide

46
Q

Examples of fibrous proteins

A

Collagen, keratin, elastin

47
Q

General structure of fibrous proteins

A

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
Q

Properties of keratin

A

Strong, inflexible, insoluble

49
Q

Function of keratin

A

To form hair, skin and nails, to help epithelial cells maintain integrity.

50
Q

Properties of collagen

A

Flexible, strong

51
Q

Function of collagen

A

To be a connective tissue in skin, tendons, ligaments and the nervous system.

52
Q

Properties of elastin

A

High resilience for large strains, low stiffness, flexible

53
Q

Function of elastin

A

To give structures like the walls of blood vessels and the lining of the lungs the flexibility to expand when needed.

Biology: Module 2: Foundations in Biology (10 decks)

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