3.7 Types of Proteins - Quaternary Proteins Flashcards

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1
Q

What type of protein is Haemoglobin?

A

Globular

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2
Q

What type of protein is Catalase?

A

Globular

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3
Q

What type of protein is Insulin?

A

Globular

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4
Q

What type of protein is Collagen?

A

Fibrous

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5
Q

What type of protein is Keratin?

A

Fibrous

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6
Q

What type of protein is Elastin?

A

Fibrous

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7
Q

Describe the structure of Haemoglobin.

A

• 4 polypeptide subunits (2 alpha, 2 beta) each wrapped around a prosthetic haem group, protecting it from being oxidised.
• When oxygen touches it, the quaternary structure changes to accommodate it.

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8
Q

What are the properties of Haemoglobin?

A
  • Fe2+ ions in haem groups can combine reversible with oxygen molecules.
  • Therefore one Haemoglobin molecule binds to 4 oxygen molecules.
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9
Q

What is the function of Haemoglobin?

A

Transports oxygen in the lungs to the cells that need it (via RBC) where it is released.

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10
Q

Describe the structure of catalase.

A

• Tetrameric enzyme containing 4 haem prosthetic groups
• Has Fe2+ ions present in prosthetic groups

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11
Q

What are the properties of Catalase?

A
  • Has Fe2+ ions which interact with hydrogen peroxide to speed up breakdown in the liver.
  • Roughly spherical shape
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12
Q

What is the function of Catalase?

A

Breaks down hydrogen peroxide in the liver. Hydrogen peroxide is a product of metabolism and is toxic to cells and cellular components when accumulated.

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13
Q

Describe the structure of insulin.

A

• 2 polypeptide chains - alpha and beta
• ^ precise shape required to fit into receptors on cell-surface membrane to take effect

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14
Q

What are the properties of insulin?

A

Water soluble (as it has to be transported in the blood stream)

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15
Q

What is the function of insulin?

A

Regulation of blood glucose concentration (initiates conversion of glucose to glycogen)

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16
Q

Describe the structure of collagen.

A

• 3 polypeptides wound together in a triple helix structure due to high proportion of glycine
• Staggered ends with cross-linking between molecules to increase strength of microfibril structure

17
Q

What are the properties of collagen?

A

Strong and flexible, insoluble in water

18
Q

What is the function of collagen?

A

Plays a structural role in the tendons, ligaments and skin.

19
Q

Describe the structure of keratin.

A

• Long stranded molecules
• 2 polypeptide chains
• High proportion of sulfur-containing amino acid cysteine
• Results in the formation of many strong disulfide bonds/bridges
• Degree of disulfide bonds determines flexibility (e.g. hair has fewer, nails have more)

20
Q

What are the properties of keratin?

A

Strong, insoluble in water, inflexible

21
Q

What is the function of keratin?

A

Plays a structural role in the hair, fingernails, skin (+horns and feathers)

22
Q

Describe the structure of elastin.

A

• Made from stretchy molecules of tropoelastin
• Long cross-linked strands containing hydrophobic regions
• These regions of different strands associate, causing molecules to group together
• When stretched, strands move apart but remain attached at cross links

23
Q

What are the properties of elastin?

A

Supple and elastic

24
Q

What is the function of elastin?

A

Plays a structural/supportive role in the skin, walls of arteries, alveoli of lungs.

25
Q

What are some common properties of globular proteins?

A

Water-soluble, spherical shape, compact, physiological function (involved in reactions)

26
Q

What are some common properties of fibrous proteins?

A

Insoluble (high concentration of hydrophobic R-groups), large number of repetitive sequences of amino acids, structural/supportive function

27
Q

What is a conjugated protein?

A

A polypeptide chain with a prosthetic group