Unit 4 Flashcards

1
Q

What is the carboxyl group on an amino acid?

A

COOH group

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2
Q

What is the amino group on an amino acid

A

NH2

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3
Q

What is the carbon skeleton on a amino acid

A

RCH

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4
Q

What are examples of aromatic amino acids

A

Tryptophan, phenylalanine, Tyrosine

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5
Q

What are nonessential (dispensable) amino acids

A

Body can make them from other AAs. (Transamination)
Can be synthesized

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6
Q

What are essential (indispensable) AAs

A

AAs that the body cannot produce enough of (must ingest)
The body cannot synthesize

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7
Q

What are conditionally essential AAs

A

Nonessential AA that becomes essential due to a certain condition (burns, liver disease, trauma)

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8
Q

How is protein digested.

A

Proteins can be denatured . Theres no enzyme to break down in the mouth, the stomach acid will also help to denature proteins (pepsin), further digested from the pancreatic proteases

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9
Q

What’s the max amount of protein you can digest at a time

A

25g

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10
Q

How is protein absorbed

A

Similar to glucose absorption, by secondary active transport through Na+ symporters

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11
Q

Why might protein not be digested as well in children

A

The barrier to break down proteins is not as developed. `

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12
Q

What triggers a food allergy

A

Immune system produces antibodies against the food triggering an anaphylactic response

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13
Q

What are risk factors of allergies

A

Genetics, cross-reactivity, inappropriate food exposures while young

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14
Q

T/F gluten is a protein in barley, Rye, and wheat

A

True

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15
Q

What causes celiac disease

A

Specific gene variant + inappropriate response to gliadin

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16
Q

T/F if someone has celiac disease its likely they have inflammation in other areas of the bod

A

True

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17
Q

What happens during transcription?

A

DNA strand replicates, Makes mRNA transcript (T becomes U), mRNA exits nucleus and travels to the ribosome

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18
Q

What is translation

A

Ribosome reads “mRNA” transcript, codon tells ribosome what AA to add next

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19
Q

What is the 2nd part of translation

A

Formation of peptide bond (dehydration reaction), synthesis of peptide chain.

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20
Q

What happens in the 3rd part of protein synthesis

A

Folding of the chains- primary to tertiary proteins.

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21
Q

What triggers insulin synthesis

A

Glucose

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22
Q

DNA error does not change the AA that is inserted.

A

Silent mutation

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23
Q

Changes to stop codon

A

Nonsense mutation

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24
Q

Insertion of wrong AA

A

Missense mutation

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25
Q

Gain or loss of base pairs (frameshift)

A

Insertion or deletion

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26
Q

What can cause protein denaturation

A

heat, pH, enzymes, agitation.

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27
Q

T/F where protein goes water follows

A

True

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28
Q

What happens when theres a lack of blood proteins

A

Water leaks into tissues and can’t be pulled back in.
Edema

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29
Q

What is proteins main function

A

Catabolism to generate ATP.

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30
Q

How does protein act as a buffer

A

It has a negative charge which allows it to accept H+ ions

31
Q

What part of the amino acid needs to be removed for gluconeogenesis

A

NH2

32
Q

What cycle helps to decrease the amount of ammonia in the blood

A

Urea cycle

33
Q

What are glucogenic AAs

A

AA carbon skeletons that can be converted to pyruvate or converted to an intermediate of the CAC

34
Q

What are ketogenic AAs

A

AA carbon skeletons that can be converted to acetyl CoA

35
Q

What is positive balance of protein

A

Eating more protein than is lost

36
Q

What is negative balance of protein

A

Losing more protein than is being replaced

37
Q

What foods contain all 9 AAs in adequate quantities

A

All animal foods
Soy, buckwheat, hemp, quinoa

38
Q

What are complementary proteins

A

2 incomplete proteins that collectively form a complete protein

39
Q

What are the health benefits of plant based diets

A

Lower LDL and total cholesterol
Lower risk of CVD, diabetes, and obesity
Lower risk of some GI cancers

40
Q

What micronutrients might someone lack on a plant based diet

A

B2, B12, D, calcium, iron, zinc

41
Q

Kwashiorkor

A

Severe acute protein malnutrition
Commonly seen after weaning
typically secondary to another issue

42
Q

Marasmus

A

Chronic protein malnutrition
Dilution/lack of infant formula
Lack of food

43
Q

At physiological pH proteins have a _______ charge

A

negative

44
Q

How would a hydrophobic side chain affect proteins

A

It will fold into the interior of the protein to avoid interacting with water in the cell

45
Q

How would a hydrophilic side chain affect the protein

A

It will face outward toward the water in the cell

46
Q

+ charge sidechain & - charge sidechain

A

These side chains will attract each other and fold together

47
Q

Where does the body obtain pyruvate

A

From glycolysis

48
Q

Where does the body obtain alpha keto glutarate

A

From the CAC

49
Q

What would happen to the pathways of macronutrient catabolism (CAC) if alpha ketoglutarate was used to synthesize glutamic acid

A

The CAC would stop since alpha-ketoglutarate is an intermediate in the CAC

50
Q

What happens in the mouth during protein digestion

A

Chewing, but no enzymatic digestion

51
Q

What happens in the stomach during protein digestion

A

Stomach acid denatures proteins, and pepsin begins proteolysis by breaking peptide bonds between adjacent AAs.

52
Q

What happens in the SI during protein digestion

A

Various proteases from the pancreas finish protein digestion by breaking them down into individual AAs

53
Q

Synthesis of an mRNA transcript from a section of DNA is called

A

Transcription

54
Q

Synthesis of a protein by reading an mRNA transcript is called

A

Translation

55
Q

If a protein is denatured which of the protein structures are lost

A

Secondary, tertiary, and quaternary

56
Q

Glucogenic/ketogenic: Cysteine, which gets converted to pyruvate

A

Glucogenic

57
Q

Glucogenic/ketogenic: Histidine which gets converted to an intermediate in the CAC

A

Glucogenic

58
Q

Glucogenic/ketogenic: Leucine which gets converted to acetyl CoA

A

Ketogenic

59
Q

Glucogenic/ketogenic: Tyrosine which gets converted to oxaloacetate

A

Glucogenic

60
Q

Gluconeogenesis takes place in

A

The liver

61
Q

Biological value

A

% of protein absorbed and incorporated into tissues

62
Q

Protein efficiency ratio

A

Ratio of weight gained to protein consumed

63
Q

Chemical score

A

Ratio of limiting amino acid to ideal amount of the amino acid in food

64
Q

PCDAAS

A

Protein digestibility multiplied by chemical score
This is the value used on food labels

65
Q

Antigen

A

Something an antibody reacts to

66
Q

Antibody

A

Immune protein that recognizes specific patterns and uses these patterns to identify the molecule as harmful

67
Q

You drink one beer. Which pathways would be responsible for metabolizing it

A

ADH

68
Q

You drink five beer. Which pathways would be responsible for metabolizing it

A

ADH
MEOS
Catalase

69
Q

The ADH mechanism takes place in

A

The cytoplasm

70
Q

What intermediate is required for the ADH pathway

A

NAD+

71
Q

What is produced in the ADH pathway

A

NADH

72
Q

What is required by the MEOS

A

NADPH
Oxygen

73
Q

What is produced by the MEOS

A

NADP+
Water