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Biology - Biological Molecules > Globular Proteins > Flashcards

Globular Proteins Flashcards

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1
Q

What does the overall 3D structure of the protein determine?

A

Which type of protein is formed

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2
Q

What are the 2 types of proteins that can be formed?

A

Fibrous

Globular

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3
Q

What are the important properties of globular proteins?

3

A

Roughly spherical in shape

Soluble in water

Very specific shapes

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4
Q

What do the roughly spherical shape of the globular have on the inside and outside?

A

Hydrophobic R groups on the inside

Hydrophilic R groups on the outside

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5
Q

What do the very specific shapes allow?

A

It allows them to carry out very specific functions

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6
Q

What are 3 roles of globular proteins?

A

Transport proteins

Hormones

Enzymes

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7
Q

What is an example of a transport protein?

A

Haemoglobin

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8
Q

What is an example of a hormone?

A

Insulin

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9
Q

What is an example of an enzyme?

A

Pepsin

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10
Q

What is the definition of a globular protein?

A

A protein with a spherical shape that is soluble in water. Globular proteins typically have metabolic roles

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11
Q

Haemoglobin

Where is haemoglobin found?

A

In red blood cells

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12
Q

Haemoglobin

What does haemoglobin have an important role in?

A

The transportation of oxygen from the lungs to the body tissues

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13
Q

Haemoglobin

What is haemoglobin made up of?

What does this mean?

A

4 polypeptide chains meaning that the protein has a quaternary structure

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14
Q

Haemoglobin

What other protein is haemoglobin also?

Why?

A

A conjugated protein

As it has a prosthetic group attached to each polypeptide chain

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15
Q

Haemoglobin

What is the definition of a prosthetic group?

A

A non-protein component that is necessary for the protein to carry out its function

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16
Q

Haemoglobin

What are the 4 prosthetic groups in haemoglobin called?

What do they contain?

A

Haem groups

They contain an iron ion (Fe2-)

17
Q

Haemoglobin

How many oxygen molecules bind to each haem group?

What does this allow?

A

One oxygen molecule

Allowing each haemoglobin to transport 4 oxygen molecules

18
Q

Insulin

What is insulin secreted by?

A

The pancreas

19
Q

Insulin

What is the important role of insulin?

A

Maintaining blood glucose concentration

20
Q

Insulin

What is insulin composed of?

(2)

A

2 polypeptide chains

An a-helix

A ß-pleated sheet

21
Q

Insulin

How are the 2 polypeptide chains joined together?

A

By disulphide links

22
Q

Insulin

What does the shape of insulin allow?

A

It to specifically bind to receptors on cell membranes to help lower blood glucose concentrations

23
Q

Insulin

What makes insulin soluble in water?

A

It has hydrophilic R groups on the outside

24
Q

Insulin

What does insulin being soluble allow?

A

It allows insulin to dissolve in the blood and be easily transported around the body

25
Q

Pepsin

What does pepsin do?

A

Catalysts the digestion of proteins

26
Q

Pepsin

Where is pepsin found?

A

In the stomach

27
Q

Pepsin

What kind of environment is the stomach?

A

An acidic environment

One with a low pH

28
Q

Pepsin

What kind of pH do many enzymes become denatured at?

(high/low)

A

At a low pH

29
Q

Pepsin

Why do many enzymes become denatured at a low pH?

A

Because they contain amino acids with basic R groups

30
Q

Pepsin

Why do enzymes that contain amino acids with basic R groups denature?

A

Basic R groups accept hydrogen ions (H+) and become positively charged

The positively charged R groups can affect the ionic bonds + hydrogen bonds in the protein - this denatures the enzyme and therefore alters its function

31
Q

Pepsin

What prevents the tertiary structure of the pepsin being affected by low pH?

A

The primary structure of pepsin has very few basic R groups

32
Q

Pepsin

How is the tertiary structure of pepsin kept stable?

(2)

A

By hydrogen bonds and disulphide links

Biology - Biological Molecules (18 decks)

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