B2.1 (proteins, from SME, 2.3.2, AI) Flashcards

1
Q

What can a protein consist of?

p

A

A protein may consist of a single polypeptide or more than one polypeptide linked together.

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2
Q

What are single polypeptide chain proteins?

A

Single polypeptide chain proteins include lysozyme, an enzyme present in mucus secretions and tears, that kills bacteria as part of our primary defences against pathogens.

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3
Q

What are proteins made up of two polypeptide chains?

A

Proteins with two polypeptide chains include insulin, a hormone responsible for regulating blood glucose levels, and integrins, a group of membrane proteins that span a phospholipid bilayer and act as a receptor.

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4
Q

What is the structure of integrins?

A

Integrins’ two polypeptide chains each have a hydrophobic section that sits in the membrane bilayer.

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5
Q

What are proteins with three polypeptide chains?

A

Proteins with three polypeptide chains include collagen, the main structural protein in skin, tendons, ligaments and the walls of blood vessels.

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6
Q

What are proteins with four polypeptide chains?

A

Proteins with four polypeptide chains include haemoglobin, which binds oxygen in red blood cells and delivers it from the lungs to respiring tissues.

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7
Q

What is a subunit in a multi-polypeptide protein?

A

Each polypeptide chain in a multi-polypeptide protein is referred to as a subunit of the protein.

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8
Q

What determines the 3D structure of proteins?

A

The amino acid sequence determines the three-dimensional conformation of a protein.

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9
Q

What is the significance of a protein’s conformation?

A

Proteins perform their diverse roles because of their 3-D shape and structure, known as the protein’s conformation.

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10
Q

How does the amino acid sequence affect protein folding?

A

The precise sequence of amino acids determines how the protein folds and aligns itself as the individual amino acids are being added at the ribosome.

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11
Q

What happens to amino acids during protein formation?

A

Amino acids are always added in the same sequence so a protein can start to form its shape even before it is fully formed.

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12
Q

What structures can form due to bonds between amino acids?

A

Bonds form between parts of amino acids that can cause a bridge to form between one part of the chain and another, creating loops, sheets, helices, and folds.

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13
Q

What can alter a protein’s 3-D shape?

A

If an amino acid is not present in its usual place in the chain due to mutation, this can drastically alter the protein’s 3-D shape and affect its function.

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14
Q

What type of protein is haemoglobin?

A

Haemoglobin is a globular protein that forms a globe-shaped structure.

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15
Q

What is the structure of collagen?

A

Collagen is a fibrous protein that has a repeating sequence of amino acids to create a helical structure.

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16
Q

What is denaturation in proteins?

A

Denaturation is the irreversible change of protein conformation caused by temperature and pH extremes.

17
Q

What causes denaturation?

A

Heat and extremes of pH are the most common causes of denaturation.

18
Q

What happens to the protein’s shape during denaturation?

A

The altered protein shape may affect its function, physical state, and general usefulness in its original role.

19
Q

Can denaturation be reversed?

A

Denaturation is almost always irreversible; the protein cannot be re-formed in its original conformation by reversing the change in conditions.

20
Q

How can small denaturations and renaturations occur?

A

Small denaturations and renaturations are possible in certain proteins to respond to small fluctuations in pH, e.g., haemoglobin.

21
Q

What is an example of denaturation in cooking?

A

Denaturation can be seen most easily by looking at the changes in an egg white as the egg is fried or poached.

22
Q

What happens to albumin during cooking?

A

Heating causes the hydrophobic amino acids in albumin to appear at the edges, causing the protein to become insoluble.

23
Q

What is the optimum pH for pepsin?

A

The stomach enzyme pepsin, a protein-digesting enzyme, has an optimum pH of 2.

24
Q

What are extremophiles?

A

Certain extremophiles have evolved to have proteins that are stable even at extreme pH or temperature, e.g., Thermus aquaticus, a bacteria that lives in hot springs at 80°C.

25
Q

Why can’t many drugs be taken orally?

A

Many drugs are proteins that cannot be taken by mouth because the protein will be denatured by stomach acid.

26
Q

What is an important tip regarding protein bonds?

A

Remember to avoid confusing the bonds that hold a protein’s shape together with the peptide bonds that attach each amino acid in sequence.