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Biology module 2 > Proteins > Flashcards

Proteins Flashcards

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1
Q

How many amino acids are there?

A

20

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2
Q

What dictates a proteins function

A

Order of amino acids the way they fold

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3
Q

What examples are there of proteins?

A

All enzymes
All antibodies
Haemoglobin

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4
Q

What makes up an amino acid?

A

An anime group (NH2)
A CH in the middle
A variable group
A carboxyl group (COOH)

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5
Q

How can you denote the variable group in amino acids?

A

With the letter R

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6
Q

What bond is formed between 2 amino acids?

A

Peptide bond

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7
Q

Describe how a dipeptide is formed

A

The amine group from 1 amino acid lines up with the carboxyl group from the other amino acid
The OH in the carboxyl group joins with a H in the amine group to form water
The N and C now can form another bond with each other (peptide bond)
This is a condensation reaction.

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8
Q

What is primary structure?

A

It is the order the amino acids join up forming a polypeptide
1000s of amino acids can join up

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9
Q

Where are polypeptides made?

A

Ribosomes and rough ER

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10
Q

What is secondary structure?

A

How the chain folds up on itself

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11
Q

What are the 2 secondary structures?

A

Alpha helix

Beta pleated sheet

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12
Q

Describe the bonding in secondary structure

A

Hydrogen bonds hold them in position

Individually they are weak but there are lots of them it is strong

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13
Q

What is tertiary structure?

A

How the polypeptide chain fold up on itself again

More complex shapes are made

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14
Q

What are the 4 bonds in tertiary structure (strongest to weakest)

A

Disulfide bond/bridge
Ionic bonds
Hydrogen bonds
Hydrophobic/hydrophilic interaction

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15
Q

Describe disulfide bonds (tertiary structure)

A

Adjacent cysteine amino acids form strong covalent bonds between sulfur

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16
Q

How do you break a disulfide bond?

A

Using a reducing agent

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17
Q

Describe ionic bonding (tertiary structure)

A

Forms between ionised amine and carboxyl groups

18
Q

How do you break the ionic bonds in tertiary structure?

A

Extreme pH

19
Q

Describe hydrogen bonding in tertiary structure

A

Forms between delta- oxygen and delta+ hydrogen

20
Q

Describe hydrophilic/hydrophobic interaction (tertiary structure)

A

Between non polar R groups
Hydrophilic go towards water (outside)
Hydrophobic go away from water (inside)

21
Q

Describe quaternary structure

A

More than 1 polypeptide joined together

Any bonds used in tertiary structure can be used

22
Q

What is a conjugated protein?

A

A protein that has a non-protein prosthetic group

23
Q

Which 3 proteins are globular?

A

Haemoglobin
Insulin
Enzymes eg catalase

24
Q

Which 3 proteins are fibrous?

A

Collagen
Keratin
Elastin

25
Q

What is the structure of haemoglobin?

A

4 chains

Contains a prosthetic haem group that contain Fe2+ ions

26
Q

What are the properties of haemoglobin?

A

Soluble

Haem group works reversibly with oxygen

27
Q

What is the function of haemoglobin?

A

Combines with oxygen/carbon dioxide and transports it in red blood cells

28
Q

Structure, properties and function of collagen

A

3 chains

Tensile strength/insoluble

Part of tendons, skin and cartilage

29
Q

Structure, properties and function of keratin

A

2 chains, disulfide bonds

Insoluble, inflexible/strong

Waterproofs cells

30
Q

Structure of insulin

A

81 amino acids

2 chains held together by disulfide bonds

31
Q

Properties of insulin

A

Soluble

Has polar groups

32
Q

Function of insulin

A

Regulates blood glucose concentration

33
Q

Structure of enzymes eg catalase

A

2000 amino acids
4 chains
Has prosthetic haem group containing Fe2+ ions

34
Q

Properties of enzymes eg catalase

A

Soluble

35
Q

Function of enzymes eg catalase

A

Breaks down hydrogen peroxide quickly

36
Q

Structure, properties and function of elastin

A

Fibrous

Stretches and recoils, insoluble

Blood vessels and alveoli contain elastin

37
Q

What makes proteins soluble?

A

Having hydrophilic/hydrophobic parts

38
Q

What are the properties of fibrous proteins?

A

Insoluble
Strong
Unreactive
Have structural roles

39
Q

What is the difference between tertiary and quaternary

A

Quaternary includes other polypeptide chains and prosthetic groups

40
Q

What are the properties of globular proteins?

A

Compact
Soluble
Have metabolic roles

Biology module 2 (19 decks)

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