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Biology Module 2 > Proteins > Flashcards

Proteins Flashcards

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1
Q

What are peptides

A

polymers made up of amino acid molecules

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2
Q

What do all proteins contain

A

carbon, hydrogen, oxygen and nitrogen

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3
Q

General structure of an amino acid

A
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4
Q

What do diff r groups result in

A

Diff amino acids

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5
Q

What is formed when 2 amino acids bond

A

Dipeptide

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6
Q

What is formed when 3 amino acids bond

A

Tripeptide

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7
Q

What is formed when many amino acids bond

A

Polypeptide

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8
Q

What type of bonds are peptide bonds

A

Covalent

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9
Q

Primary structure of a protein

A

sequence of amino acids joined by peptide bonds

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10
Q

What determines the primary structure of proteins

A

DNA

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11
Q

Secondary structure of proteins

A

occurs when the sequence of amino acids are linked by hydrogen bonds in an alpha helix or beta helix pleated sheet

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12
Q

What interacts to form the secondary structure

A

the weak negatively charged nitrogen and oxygen atoms interact with the weak positively charged hydrogen atoms to form hydrogen bonds

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13
Q

What type of bonds make up the secondary structure

A

Hydrogen bonds

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14
Q

What type of protein mostly has a secondary structure

A

Most fibrous proteins

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15
Q

What can hydrogen bonds be broken by in the secondary structure

A

High temp and pH changed

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16
Q

Tertiary structure

A
  • folding of polypeptide chains determined by
    Hydrogen bonds
    Disulphide bonds
    Ionic bonds
    Weak hydrophobic interactions
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17
Q

What protein is tertiary structure common in

A

Globular

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18
Q

What type of bond is a disulphide bond

A

Covalent bond

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19
Q

What does disulphide bonds form between

A

two cysteine R groups

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20
Q

Strongest r group interaction

A

Disulphide

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21
Q

What can disulphide bonds be broken by

A

Oxidation

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22
Q

What are ionic bonds broken by

A

pH change

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23
Q

What is the quaternary structure in a protein

A

Two or more polypeptide chains being joined together

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24
Q

Example of a protein w a quaternary structure

A

Haemoglobin

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25
Q

Globular proteins properties

A

Soluble, spherical, 3D, pH sensitive, hydrophilic outside

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26
Q

Globular proteins functions

A
  • metabolic role within body
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27
Q

Fibrous protein properties

A

Insoluble
Elongated
Strong
Flexible

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28
Q

Fibrous proteins functions

A
  • structural role within body
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29
Q

What is a conjugated protein

A
  • contains non protein group
  • has prosthetic group attached by covalent bonds
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30
Q

Examples of conjugated proteins

A

Haemoglobin, catalase

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31
Q

What prosthetic group does haemoglobin have

A

Haem

32
Q

Haemoglobin

A
  • quaternary structure
  • 2 a-globin, 2 b-globin chains
  • 4 haem groups
  • found in red blood cells
  • globular protein
33
Q

What do haem groups contain + why

A

Iron which bonds to the oxygen

34
Q

How many oxygen molecules can one haemoglobin molecule transport

A

4

35
Q

How does haemoglobin work

A
  • oxygen is transported to the cells which need it and it is released
  • transport substances in blood
36
Q

Catalase

A
  • globular protein
  • quaternary protein containing 4 haem prosthetic groups
37
Q

What is catalase

A

Enzyme = speeds up rate of chemical reactions without being used up

38
Q

What does catalase do

A

Breaks down hydrogen peroxide into water and oxygen

39
Q

What is catalase’s prosthetic group

A

Iron II ions

40
Q

What do iron II ions in catalase allow

A

Allow catalase and hydrogen peroxide to interact which speeds up hydrogen peroxide’s breakdown

41
Q

Insulin

A
  • globular protein
  • quaternary structure = 1 alpha chain and 1 beta chain
  • contains disulphide bonds l
42
Q

Insulin solubility + benefit

A

Soluble in water = can be transported by the blood

43
Q

What is insulin involved in

A

Hormone involved in the regulation of blood glucose concentration

44
Q

Why does insulin have a precise shape

A

To fit into specific receptors on cell surface membranes to cause more/less glucose production

45
Q

Collagen

A
  • fibrous protein
  • few hydrophilic r groups, mainly hydrophobic
46
Q

Amino acid pattern collagen

A

Every 3rd amino acid is glycine

47
Q

Collagen function

A

For structure
Gives mechanical strength + prevents bursting and stretching
Can be used to make up bones and tendons

48
Q

Where is collagen found

A

In artery walls = Connective tissue

49
Q

What is keratin and where’s it found

A
  • fibrous protein
    Found in hair, nails, skin and feathers
    Used for protection
50
Q

Bonds in keratin + benefiting

A
  • disulphide bonds = makes keratin strong, flexible and insoluble
51
Q

Benefit of keratin’s solubility

A

Insoluble = impermeable to water so it’s the primary protection against pathogens

52
Q

What is elastin and where’s it found

A
  • fibrous protein in elastic fibres
  • found in walls of blood vessels and alveoli of lungs
53
Q

Function of elastin

A
  • gives elasticity = allows these structures to stretch when needed
54
Q

Structure of elastin

A

Quaternary structure
Made up of tropoelastin

55
Q

Amino acids in elastin

A

1/3 amino acids are glycine = random distribution +hydrophobic

56
Q

Benefit of elastin’s hydrophobic quality

A
  • allows elastin molecules to slide over each other or stretch
57
Q

Collagen bonds

A
  • many hydrogen bonds
  • many covalent bonds
58
Q

Describe and explain why collagen is a fibrous protein

A
59
Q

Purpose of iron II ion in haemoglobin

A

able to reversibly combine with an oxygen molecule forming oxyhaemoglobin and results in the haemoglobin appearing bright red

60
Q

Where is insulin produced

A

Pancreas

61
Q

Why must insulin be soluble

A

Hormone transported in bloodstream

62
Q

Collagen properties

A

forms connective tissue
•strong + tensile strength
• stable
• insoluble

63
Q

Why does collagen have great tensile strength

A

presence of the many hydrogen bonds within the triple helix structure of collagen results in great tensile strength.

64
Q

Why is collagen strong

A

Many hydrogen and covalent bonds

65
Q

Why’s collagen insoluble

A

The length of collagen molecules means they take too long to dissolve in water

66
Q
A
67
Q
A
68
Q
A
69
Q
A
70
Q
A
71
Q
A
72
Q
A
73
Q
A
74
Q

ii

A
75
Q

How do hydrogen bonds occur in alpha helix

A

each NH forms hydrogen bonds with C=O (3-4 amino acids apart in the same polypeptide chain)

76
Q

How do hydrogen bonds occur in beta pleated sheet

A

each NH forms hydrogen bonds w C=O on adjacent parts of the same polypeptide chain

77
Q

What are bonds between in the tertiary structure

A

Hydrogen bonds between R groups w C=O from the carboxyl group and the NH from the amide group
Ionic bonds between R groups that are charged
Hydrophobic interactions between non polar R groups
Hydrophilic interactions between polar R groups

Biology Module 2 (11 decks)

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