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Biology Module 2 > Proteins > Flashcards

Proteins Flashcards

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
Globular proteins properties
Soluble, spherical, 3D, pH sensitive, hydrophilic outside
26
Globular proteins functions
- metabolic role within body
27
Fibrous protein properties
Insoluble Elongated Strong Flexible
28
Fibrous proteins functions
- structural role within body
29
What is a conjugated protein
- contains non protein group - has prosthetic group attached by covalent bonds
30
Examples of conjugated proteins
Haemoglobin, catalase
31
What prosthetic group does haemoglobin have
Haem
32
Haemoglobin
- quaternary structure - 2 a-globin, 2 b-globin chains - 4 haem groups - found in red blood cells - globular protein
33
What do haem groups contain + why
Iron which bonds to the oxygen
34
How many oxygen molecules can one haemoglobin molecule transport
4
35
How does haemoglobin work
- oxygen is transported to the cells which need it and it is released - transport substances in blood
36
Catalase
- globular protein - quaternary protein containing 4 haem prosthetic groups
37
What is catalase
Enzyme = speeds up rate of chemical reactions without being used up
38
What does catalase do
Breaks down hydrogen peroxide into water and oxygen
39
What is catalase’s prosthetic group
Iron II ions
40
What do iron II ions in catalase allow
Allow catalase and hydrogen peroxide to interact which speeds up hydrogen peroxide’s breakdown
41
Insulin
- globular protein - quaternary structure = 1 alpha chain and 1 beta chain - contains disulphide bonds l
42
Insulin solubility + benefit
Soluble in water = can be transported by the blood
43
What is insulin involved in
Hormone involved in the regulation of blood glucose concentration
44
Why does insulin have a precise shape
To fit into specific receptors on cell surface membranes to cause more/less glucose production
45
Collagen
- fibrous protein - few hydrophilic r groups, mainly hydrophobic
46
Amino acid pattern collagen
Every 3rd amino acid is glycine
47
Collagen function
For structure Gives mechanical strength + prevents bursting and stretching Can be used to make up bones and tendons
48
Where is collagen found
In artery walls = Connective tissue
49
What is keratin and where’s it found
- fibrous protein Found in hair, nails, skin and feathers Used for protection
50
Bonds in keratin + benefiting
- disulphide bonds = makes keratin strong, flexible and insoluble
51
Benefit of keratin’s solubility
Insoluble = impermeable to water so it’s the primary protection against pathogens
52
What is elastin and where’s it found
- fibrous protein in elastic fibres - found in walls of blood vessels and alveoli of lungs
53
Function of elastin
- gives elasticity = allows these structures to stretch when needed
54
Structure of elastin
Quaternary structure Made up of tropoelastin
55
Amino acids in elastin
1/3 amino acids are glycine = random distribution +hydrophobic
56
Benefit of elastin’s hydrophobic quality
- allows elastin molecules to slide over each other or stretch
57
Collagen bonds
- many hydrogen bonds - many covalent bonds
58
Describe and explain why collagen is a fibrous protein
59
Purpose of iron II ion in haemoglobin
able to reversibly combine with an oxygen molecule forming oxyhaemoglobin and results in the haemoglobin appearing bright red
60
Where is insulin produced
Pancreas
61
Why must insulin be soluble
Hormone transported in bloodstream
62
Collagen properties
forms connective tissue •strong + tensile strength • stable • insoluble
63
Why does collagen have great tensile strength
presence of the many hydrogen bonds within the triple helix structure of collagen results in great tensile strength.
64
Why is collagen strong
Many hydrogen and covalent bonds
65
Why’s collagen insoluble
The length of collagen molecules means they take too long to dissolve in water
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ii
75
How do hydrogen bonds occur in alpha helix
each NH forms hydrogen bonds with C=O (3-4 amino acids apart in the same polypeptide chain)
76
How do hydrogen bonds occur in beta pleated sheet
each NH forms hydrogen bonds w C=O on adjacent parts of the same polypeptide chain
77
What are bonds between in the tertiary structure
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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