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Medical biochemistry > Protein > Flashcards

Protein Flashcards

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USMLE® Step 1 flashcards
1
Q

Why is protein important?

A

Mediate most of the actions of life –> critical to all life processes.

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2
Q

What is dependent upon protein:

A

Structure and activity; growth, development, and continued maintenance of systemic tissues.

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3
Q

Protein synthesis:

A

The body’s need for protein met trough food –> protein synthesis in the liver

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4
Q

How many proteins must be synthesized to varry out the body’s activities?

A

50 000 different proteins.

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5
Q

What is the most abundant protein in the body?

A

Collagen –> found in all connective tissues.

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6
Q

What is enzymes?

A

Proteins that serve as chemical catalyst –> speeding up chemical reactions.

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7
Q

What can transport proteins do?

A

Shuttle chemical elements, such as oxygen (haemoglobin) or store minerals, such as iron (ferritin)

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8
Q

Why is antibodies important?

A

To maintain a healthy immune system.

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9
Q

What is the main role of protein?

A

Tissue building

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10
Q

What are protein made up of?

A

Amino acids

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11
Q

Amino acid structure:

A

Amino group (NH2), acid group (COOH), central carbon (C), side chain

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12
Q

Protein differ from:

A

Carbohydrates and fats –> presence of the amino groups.

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13
Q

What does Amino Acids have?

A

Amino group, carboxyl group and R-group attached to the same carbon.

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14
Q

What is Dipeptides

A

2.enzym: Aspartame (artifical sweetener)

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15
Q

What is Tripeptides?

A

3.enzym: Glutathione (natural antioxidant)

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16
Q

Short polypeptides?

A

Peptide hormones (glucagon)
Neurotransmitters (Substance)

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17
Q

Large polypeptides?

A

Proteins

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18
Q

Large proteins?

A

Dystrophin

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19
Q

How does proteins differ?

A

Number, order or sequencing.

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20
Q

How are the 20 amino acids categorized?

A

Required to be present in the diet or can be synthesized in the liver for other amino acids.

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21
Q

How are amino acids termed?

A

Essential (indispensable) and non-essential (dispensable) amino acids.

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22
Q

Protein structure: 4 levels

A

Primary, secondary, tertiary (3D) and quaternary

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23
Q

Sequence of aa in peptide chain

A

Primary structure

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24
Q

Folding/coiling of peptide chain: alfa - helix or beta-pleated sheet.

A

Secondary structure

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25
Q

Peptide chain folds upon itself

A

Tertiary (3D) structure

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26
Q

Folded peptide chains join together

A

Quanternary structure.

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27
Q

What happens when protein is eaten as part of the diet.

A

It is not absorbed directly, but must be broken down into component amino acids.

28
Q

What is stage 1

A

Digestion in the mouth

29
Q

Where does digestion begins?

A

In the mouth with the moistening effect of saliva and the chewing by the teeth.

30
Q

What is secreted by parietal cells in the smomach lining?

A

Hydrochloric acid (HCl)

31
Q

Why is HCl secreted?

A

To denature the protein and provide an environment for digestion.

32
Q

What does chief cells in the stomach lining produce?

A

An inactive enzyme, pepsinogen.

33
Q

What does the acidic environment converts the pepsinogen to ?

A

The active protease (proteincleaving enzyme), pepsin.

34
Q

What breaks the polypeptide chain at numerous sites?

A

Pepsin

35
Q

Where does the breakdown of the polypeptides takes place?

A

In a small intestine

36
Q

What is absorbed by the small intestine?

A

Amino acids and short peptides

37
Q

Where is proteins transported when proteins are degraded to amino acids and absorbed into the bloodstream.

A

To the liver which is the site of amino acid synthesis.

38
Q

Why is a small percentage of amino acids broken down?

A

To provide energy

39
Q

Why are protein intake, maintenance, metabolism and losses are carefully regulated?

A

Because protein is so important.

40
Q

What is the name of the procedure where body proteins are degraded to amino acids and re-synthesized?

A

Protein turnover

41
Q

What is the average protein turnover in adult?

A

300-400 g per day

42
Q

What do we call food with high protein concentration?

A

“Protein foods”

43
Q

What is protein rich foods?

A

Meat, fish, milk, cheese, eggs and legumes.

44
Q

What do we call amino acid that are rapidly catabolised and the nitrogen is excreted as urea in the urine.

A

Surplus amino acids.

45
Q

What is defined as the protein source’s ability to support growth?

A

Protein quality

46
Q

What do we call a protein that has all the essential amino acids present in proper proportions to substain growth?

A

A complete protein

46
Q

What do we call a protein that has all the essential amino acids present in proper proportions to substain growth?

A

A complete protein (high biological value)

47
Q

Example of a protein that are incomplete?

A

Plant based

48
Q

What do we call a protein that has high biological value?

A

Complete protein

49
Q

What do we call a protein that has low biological value?

A

Incomplete proteins

50
Q

What effects on calcium metabolism?

A

High-protein diets.

51
Q

What happens when protein increases in the diet.

A

Bone loss

52
Q

What effects on calcium metabolism

A

High-protein diets.

53
Q

What can excessive intake lead to?

A

Lead to deterioration of renal function in patients with chronic renal disease (stages 1-4)

54
Q

Who are at high risk of protein malnutrition (muscle loss)?

A

People that are chronically ill and elderly people.

55
Q

What is a serious concern for childern in developing countries.

A

Protein-energy malnutrition.

56
Q

Matrix protein of skin, bones and teeth

A

Collagen

57
Q

Oxygen transport

A

Haemoglobin

58
Q

Iron storage

A

Ferritin

59
Q

Catalyzes the breakdown of starch to sugar in the mouth

A

Salivary amylase

60
Q

Digest protein in the stomach

A

Pepsin

61
Q

A hormone that regulates uptake and storage of glucose

A

Insulin

62
Q

Found in salvia that neutralize foreign substance

A

IgA antibodies

63
Q

How much percent should calories come from fat?

A

30-33%

64
Q

How much percent saturated fat intake should be?

A

<10%

65
Q

Fat around the organs

A

Visceral fat

66
Q

What do not contain nitrogen?

A

Water, fat and carbohydrates

Medical biochemistry (9 decks)

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