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Metabolism in Human Nutrition > Proteins n shit > Flashcards

Proteins n shit Flashcards

1
Q

What configuration do most amino acids have?

A

L-form

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2
Q

What amino acid doesn’t have L-form configuration?

A

Glycine

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3
Q

What amino acid is not an alpha amino acid?

A

Proline

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4
Q

What does the formation of a peptide bond require?

A

The elimination of water

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5
Q

What is the primary structure of a protein?

A

The order of amino acids in a polypeptide

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6
Q

How many amino acids are used for protein synthesis?

A

20

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7
Q

How many amino acids have hydrophilic side chains?

A

9

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8
Q

How many amino acids have hydrophobic side chains?

A

8

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9
Q

What amino acid has an H side group?

A

Glycine

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10
Q

What amino acid has an SH side group

A

Cysteine

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11
Q

Name an imino acid

A

Proline

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12
Q

What amino acids have acidic side chains?

A

Aspartate and glutamate

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13
Q

What amino acids have basic side chains?

A

Lysine, arginine, and histidine

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14
Q

What is the secondary structure of a protein?

A

Describes the local folding of a polypeptide chain

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15
Q

In alpha helices, what way do the chains turn? Why is this?

A

Right handed; because most proteins contain L amino acids

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16
Q

How many amino acids are in each turn?

A

3.6 amino acids

17
Q

Give two examples of amino acids which favour the formation of alpha helices

A

Methionine and leucine

18
Q

Give one example of an amino acid which does not favour the formation of alpha helices

A

Proline

19
Q

What is tertiary structure?

A

Describes the overall arrangement of amino acids in 3D

20
Q

What is quaternary structure?

A

Occurs when two or more polypeptide chains interact with one another

21
Q

What is a protein domain?

A

It is a region within a larger protein that themselves are stable and self-contained

22
Q

How can proteins evolve?

A

By recombination of protein domains

23
Q

What type of protein is hair made from?

A

Alpha keratin

24
Q

What is collagen made up of?

A

Tropocollagen; contains the modified amino acids hydroxyproline and hydoxylysine

25
Q

Describe the structure of myoglobin

A

It is a monomeric protein. Made up of alpha helices and connecting loops with a molecule of haem bound to it

26
Q

What has a higher affinity for oxygen: haemoglobin or myoglobin?

A

Myoglobin

27
Q

Describe the structure of haemoglobin

A

Is a tetramer of polypeptide chains, 2 alpha and 2 ß subunits. Each has a molecule of haem bound to it.

28
Q

What are the two models of homotropic cooperativity?

A

The concerted and sequential models

29
Q

What effect does 2, 3-biphosphoglycerate have on the oxygen binding curve?

A

Shifts it to the right (ie decrease affinity of haemoglobin for oxygen)

Metabolism in Human Nutrition (5 decks)

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