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KIN 275 > Module 6 - Proteins > Flashcards

Module 6 - Proteins Flashcards

1
Q

How much of the human body is protein?

A

15%

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2
Q

Protein deficiency is common in Canada: T or F?

A

False. Protein deficiency is rare in Canada. Most people have more then the AMDR recommends.

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3
Q

About what percent of Canadians consume over 10% AMDR of protein?

A

> 97%

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4
Q

What is the AMDR for Protein for adults?

A

10-35%

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5
Q

On average, how much of total kcal is from protein?

A

15%

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6
Q

What are the pros and cons of protein from animal sources?

A

Pros: Great source of B vitamins and minerals (iron, zinc, calcium)
Cons: Low in Fibre, usually high in SFA and cholesterol

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7
Q

What are the pros and cons of protein from plant sources?

A

Pros: Good source of most B vitamins and minerals (iron, zinc, calcium) contains fibre, unsaturated fats
Cons: Less absorbable forms of iron, zinc, calcium present

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8
Q

Name Similarities and Differences between Proteins and Carbohydrates, Fats

A

Similarities:
- Made in body and consumed in various forms
Differences:
- proteins are made according to instructions from DNA
- proteins contain N along with CHO

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9
Q

What are amino acids?

A

nitrogen containing molecules
that combine to form proteins

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10
Q

What are proteins?

A

Chains of amino acids in different sequences

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11
Q

How long is a Dipeptide?

A

2 amino acids

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12
Q

how long is a Tripeptide?

A

3 amino acids

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13
Q

How long is a oligopeptide?

A

4-9 amino acids

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14
Q

How long is a polypeptide?

A

10+ (many peptide bonds)

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15
Q

How many amino acids in a protein?

A

more than 50 amino acids

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16
Q

How many amino acids typically in a protein?

A

between 100-10,000 amino acids in a sequence

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17
Q

What processes synthesize and break down proteins?

A

Synthesize: Condensation
Break down: Hydrolysis

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18
Q

What are peptide bonds?

A

chemical bond between carboxyl group of one amino acid and amine group of another amino acid

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19
Q

What parts of the amino acids bind together in condensation?

A

amine group and carboxyl group (acid group)

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20
Q

How many unique amino acids are there?

A

20

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21
Q

What are the components of an amino acid?

A

Central carbon
Hydrogen
Acid/Carboxyl Group (COOH)
Amino Group (NH2)
Unique Side Group (R)

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22
Q

By combining the 20 amino acids in various lengths and sequences, the body is able to make

A

10,000 - 50,000 unique proteins

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23
Q

How many of the 20 amino acids are “essential”/”indispensable”?

A

9

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24
Q

How many of the 20 amino acids are “non-essential”/”dispensable” or conditionally essential?

A

11

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25
Q

Non-essential amino acids are less important then essential amino acids: T or F?

A

False. non essential AAs are just as important as essential AAs, however our body makes non-essential AAs so they are of less concern in diet

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26
Q

What are essential Amino Acids?

A

amino acids that body does not make

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27
Q

what are conditionally essential amino acids?

A

amino acids that are not synthesized at a rate to meet body’s needs

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28
Q

How are non-essential and conditionally essential amino acids synthesized in the body?

A

Transamination: involves transfer of amino group to a compound which creates new amino acid

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29
Q

What are the characteristics that differentiate amino acid chains?

A
  1. Number of amino acids
  2. Proportion of each amino acid
  3. Order of amino acids
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30
Q

Chains of amino acids fold into specific way, giving each protein a unique 3D shape that is essential to its function: T or F?

A

True. Proteins can fold due to bonds linking amino acids together and become 3D. Structure = Function.

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31
Q

Is insulin a protein?

A

Yes! Discovered by Canadian Frederick Banting and produced in the pancreas by Beta cells to regulate high blood sugar.

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32
Q

How is protein structure formed?

A

polypeptide chains fold and may bind together. The structure determines the function.

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33
Q

How does the structure of hemoglobin protein determine its function?

A

spherical shape allows for places for heme (a non protein portion of hemoglobin) to hold and transport iron

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34
Q

What are ways in which the structure and therfore function of proteins are changed?

A
  1. Mutation
  2. Denaturation
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35
Q

What is mutation?

A

alteration of gene sequence that codes for specific proteins

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36
Q

What is an example of mutation in protein?

A

sickle cell anemia, changes shape of blood cell to “sickle”, changing function

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37
Q

The polypeptide protein chains found in hemoglobin of sickle cell anemic individual will be different then someone without sickle cell anemia: T or F?

A

True. They are mutated, as a single AA is altered, causing protein molecules to bind together in long chains. This causes a distorted shape, unlike the normal disc shape of RBC. Alters ability to release and carry 02, dangerous.

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38
Q

What is Denaturation? How does it occur?

A

uncoiling of proteins which causes loss of shape. Occurs when protein exposed to heat, acids, bases, heavy metals, alcohol etc.

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39
Q

What is an example of protein denaturation?

A

stiffening of egg whites
salt on meat, denatures the protein to make juicer meat

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40
Q

Denaturation of proteins in digestion allows…

A

for breakdown into amino acids and absorption

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41
Q

How does digestion in the mouth differ for proteins compared to CHO and lipids?

A

no enzymatic digestion for proteins in mouth (CHO have salivary amylase to break them down and fats are broken down by lingual lipase)

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42
Q

Explain how protein digestion begins in the stomach?

A

HCL and pepsin begin chemical digestion of protein in the stomach

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43
Q

What cells secrete pepsinogen in the stomach?
What cells secrete HCL in the stomach?

A

Chief cells secrete pepsinogen
Parietal cells secrete HCL

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44
Q

Explain the denaturation of proteins in the stomach through parietal cells and chief cells?

A

Parietal cells release HCL which begin denaturation of proteins, they also activate the pepsinogen from chief cells to become pepsin, a protein that breaks peptide bonds

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45
Q

Explain the role of the pancreas in digesting proteins?

A

Pancreas releases protein digesting enzymes into duodenum (mixing bowl) of the small intestine which breakdown amino acids

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46
Q

What enzymes are released by pancreas into small intestine for protein digestion?

A

Trypsin and Chymotrypsin
Trypsin activates chymotrypsin and they both can cleave peptide bonds

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47
Q

A lot of protein is lost in feces: true or false?

A

FALSE, very little protein is lost in feces, most is absorbed in the duodenum and jejunum of the small intestine.

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48
Q

Where do amino acids go after entering mucosal cell and proceeding to blood?

A

To the liver, which distributes to the rest of the body.

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49
Q

Where is most of protein absorbed?

A

Small intestine, by the pancreatic enzymes trypsin, chymotrypsin and brush border enzymes

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50
Q

What is role of pepsin in stomach protein digestion?

A

breaks protein apart

51
Q

Proteins are absorbed in the form of ___ ___ through specific carriers

A

amino acids

52
Q

Explain the co-transport of amino acids, dipeptides or tripeptides across intestinal epithelial cell

A

1 Na+ is required in co-transport of each amino acid, dipeptide or tripeptide through to the blood stream and eventually the liver

53
Q

Food allergies are triggered when…

A

a whole protein is absorbed without being digested

54
Q

A rapid, severe allergic reaction is called…

A

Anaphylaxis

55
Q

Why are people with GI disease prone to allergic reactions?

A

Their damaged intestines allow for the digestion of whole proteins

56
Q

Amino acids in body tissues and fluids are referred to collectively as the

A

amino acid pool

57
Q

What accessory organ is in charge of distribution of amino acids throughout the body

A

Liver

58
Q

Proteins required for synthesis come from…

A

amino acid pool

59
Q

Where are instructions for specific proteins contained?

A

DNA

60
Q

Chromosomes contain ___ that stores ___ for protein synthesis

A

DNA
Genetic instructions

61
Q

Genetic information flows through the central dogma which is…

A

DNA > RNA > Protein

62
Q

What process turns DNA into RNA?

A

Transcription

63
Q

What process turns RNA into Protein?

A

Translation

64
Q

Explain Protein Turnover

A

Fact that proteins are always being degraded and synthesized

65
Q

Do structural proteins (eg. collagen) have slower or faster rates of protein turnover?

A

Slower

66
Q

What is an example of quick Protein Turnover?

A

Insulin, can be increased in amount rapidly by increasing synthesis and decreasing degradation, and decreased by doing the reverse.

67
Q

If the protein to be made requires more of a certain amino acid then is available, said amino acid is a…

A

limiting amino acid (as it limits protein synthesis)

68
Q

What is transamination?

A

process used to synthesize nonessential amino acids (transfer of amine group)

69
Q

What is Deamination?

A

Removal of amine group to synthesize other nitrogen containing compounds

70
Q

Nitrogen from amino acids can be removed (in deamination) to form other nitrogen-containing compounds such as:

A

Neurotransmitters
Phosphatidylcholine (lecithin)
Hormones

71
Q

Deamination produces 3-carbon molecules that can be used to…

A

synthesize glucose

72
Q

Deamination produces 2-carbon molecules that form

A

acetyl-CoA for ATP production

73
Q

When protein and energy are excess, amino acids converted to acetyl-CoA via deamination are used to…

A

synthesize fat for storage

74
Q

Deamination is…

A

the removal of amino group (NH2) from amino acid

75
Q

What is the toxic waste product formed by Deamination?

A

Ammonia

76
Q

What happens to ammonia (toxic waste product) formed by Deamination?

A

Liver combines ammonia with CO2 to form Urea which is released into bloodstream and filtered by kidney for excretion in urine (UREA is URINATED)

77
Q

Kidneys need water to excrete Urea, if there is no water, what happens?

A

Water is taken from body water

78
Q

Excess urea (or ammonia) in blood does what?

A

changes PH

79
Q

What does the process of deamination and its production of toxic waste product mean for high protein diet?

A

When on high protein diet, water intake must be increased drastically or else you will risk dehydration. More protein intake means more Ammonia from deamination which along with CO2 takes the form of Urea and therefore more urination.

80
Q

What is hyperammonemia?

A

Too much ammonia, toxic, occurs through deamination

81
Q

As nitrogen is secreted via Urea (there is nitrogen in Ammonia), we can use the balance of N in the body to assess protein intake: State the equation for N balance

A

N balance: N (g) intake - N (g) output

82
Q

If N balance is + then…

A

Protein synthesis > breakdown

83
Q

If N balance is - then…

A

Protein breakdown > synthesis

84
Q

Name at least 3 ways Nitrogen can be lost in the body

A

Urine (Urea, Ammonia) - major way
Feces - major way
Dermal (skin debris, sweat) - minor way
Hair, Nails - minor way

85
Q

If Dietary N intake > N loss/excretion then..

A

there is enough nitrogen to support growth and repair

86
Q

How/when does a positive N balance happen?

A

When you eat more protein then required for body’s maintenance

87
Q

How/when does a negative N balance happen?

A

Inadequate protein intake

88
Q

Name at least 3 functions of proteins

A

Structure
Enzymes
Hormones
Transport
Contraction
Water balance
Buffering
Protection & Defense
Detoxification
Source of energy & glucose

89
Q

How does protein provide structure in the body?

A

Eg. Collagen holds together cells and forms protein framework of bones and teeth, also forms ligaments and tendons

90
Q

How are proteins involved as enzymes in the body?

A

protein enzymes speed up metabolic reactions

91
Q

How are proteins involved in hormones in the body?

A

some hormones are made of amino acids, they are called peptide hormones (insulin and glucagon)

92
Q

How are protein hormones different then steroid hormones?

A

Peptide hormones bind to protein receptors on surface of cell membrane while steroid hormones diffuse through cell membrane to enter cell

93
Q

How are proteins involved in transport in the body?

A

Proteins transport substances all over the body, and sometimes even in and out of cells. Eg. Glucose is transported by carrier proteins across cell membrane
Another Eg. Hemoglobin transports oxygen from lung to tissues

94
Q

How is protein involved in contraction?

A

proteins in muscles allow for contractions

95
Q

How does protein play a role in water balance in the body?

A

protein exerts oncotic pressure (pushes water into blood from intercellular space)
- when blood protein is low, more water is pushed into intercellular spaces and fluid accumulates leading to edema

96
Q

How does protein play the role of a buffer in the body?

A

some amino acids can resist change of pH due to acid, maintaining balance by donation and acceptance of H+
Normal blood pH is 7.4
pH<7.35 acidosis sets in and can cause coma
pH>7.45 alkalosis can result in convulsions

97
Q

How does protein protect and defend the body?

A
  • it is the main component of skin
  • when foreign particles enter, proteins called antibodies are formed to eliminate foreign particle
    adequate protein is important for these AA to function
98
Q

How does protein detoxify the body?

A

Liver enzymes (which are proteins) detoxify toxins
inadequate protein reduces ability to detoxify such compounds

99
Q

How is protein a source of energy and glucose?

A

protein can be sacrificed to produce energy and glucose (gluconeogenesis) in absence of CHO and fat

100
Q

What two factors determine the quality of a protein?

A
  1. amino acid composition
  2. digestibility
101
Q

What is a complete protein?

A

dietary protein which contains all 9 essential amino acids in adequate amounts for human use

102
Q

Where can you get complete proteins?

A

all animal products (except gelatin) are complete

103
Q

What is an incomplete protein?

A

dietary protein which lacks or contains limited amounts of essential amino acids; could not support growth if sole source of protein

104
Q

What are complimentary proteins?

A

2 or more proteins that together allow you to have each essential amino acid (but individually they do not have each essential amino acid)

105
Q

What is an example of complimentary protein?

A

black beans and rice

106
Q

What is the purpose of the DIAAS %?

A

it shows how much of the amino acids in a certain food will actually be absorbed

107
Q

What products typically score well on DIAAS and PDCAA rankings?

A

animal products like chicken, eggs, meat and milk

108
Q

What is the AMDR for protein in a day?

A

10-35% of total energy

109
Q

What is the RDA for protein for adults?

A

0.8g protein/kg of body mass

110
Q

Is there a UL for protein?

A

No, but caution against consuming additional AA above what is found in food

111
Q

What life stages would require more protein?

A

Elderly (due to age related muscle loss)
Pregnant woman
Children

112
Q

How much muscle do we lose each year after age 40?

A

about 1% of our muscle each year (sarcopenia)

113
Q

The RDA for protein of 0.8g/kg of body weight is a great guideline for everyone regardless of age, lifestyle, to use: true or false?

A

False, based on studies over 50 years ago for healthy young adults

114
Q

What are the possible negative effects of excess protein?

A

obesity, heart disease, cancer and osteoporosis (calcium excretion associated with high protein)

115
Q

Diets higher in protein are also usually higher in ___

A

saturated fats and cholesterol (dietary cholesterol has little effect on blood cholesterol)

116
Q

Why can amino acid supplements such as protein powder be dangerous?

A

they could lead to imbalance of AA and overload of some AA while others are neglected

117
Q

What is the problem with being especially high in some AAs?

A

amino acids compete to go through same protein channels sometimes, so more abundant amino acid will become more present in cell while other amino acid is less present

118
Q

DIAAS vs PCDAAS

A

DIAAS: samples protein from ileum
PCDAAS: samples proteins from feces (assumes if AA is not there it was digested)

DIAAS is better and more accurate representation of amino acid digestion in humans

119
Q

Are smaller peptides and amino acids absorbed into mucosal cell with active or passive transport?

A

Active

120
Q

AMINO ACIDS can be used to provide energy: true or false?

A

True, but it is not the first choice of energy of the body.

121
Q

High protein diets increase production of ___

A

Urea and other waste products (which can cause dehydration), increase Ca+ loss, can be high in saturated fats or cholesterol

122
Q

To meet protein needs you should:

A

have N balance, AMDR of 10-35%, have a variety of animal and plant proteins

123
Q

Loss of calcium is linked to

A

osteoporosis

KIN 275 (13 decks)

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