Protein Structure and Function Flashcards

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1
Q

Where are the H bonds in an alpha helix?

A

In the same polypeptide (backbone, not side chains)

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2
Q

Is an alpha helix right or left handed?

A

Right

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3
Q

How many amino acids are there per turn in an alpha helix?

A

3.6

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4
Q

Explain the H bonding in a beta pleated sheet

A

Formed between peptide chains and hold strands together

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5
Q

What are the two types of beta pleated sheets? Which is more common in globular proteins/

A

Parallel and antiparallel. Antiparallel are more common.

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6
Q

What percentage of haemoglobin are alpha helixes?

A

60%

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7
Q

What is a super - secondary structure?

A

Combinations of alpha helixes and beta sheets

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8
Q

What happens to hydrophobic regions in proteins due to their inability to form H bonds?

A

The regions fold in a way to minis the contact with aqueous environment.

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9
Q

What are the 3 types of post - translational modifications to proteins?

A
  1. Glycosylation (addition of sugar)
  2. Phosphorylation (cell signalling and change in activity of enzymes)
  3. Methylation/acetylation of NH2 groups in side chains
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10
Q

What is the most abundant protein in vertebrates?

A

Collagen

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11
Q

What modified amino acids does collagen contain?

A

Hydroxyproline and hydroxlsyine

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12
Q

Glycine appears every 3 amino acids in collagen. Why is this important?

A

Only has a H as an R group which means that the proteins can pack closely together.

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13
Q

How many chains does collagen have? How many amino acids per turn? What type of helix is each chain?

A

3 and 3 and a left - handed helix

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14
Q

What do the 3 chains in collagen fold to make?

A

A right handed super helix

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15
Q

How many collagen types are there and what percentage of collagen does type 1 make up?

A

25 types and this makes up 90%

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