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Nutrition Exam 2 > Chapter 6: Proteins > Flashcards

Chapter 6: Proteins Flashcards

1
Q

proteins are

A

macronutrients

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2
Q

how many kcals/g are proteins

A

4 kcals/g

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3
Q

protein involvement in enzymes

A

all enzymes are made of proteins

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4
Q

protein involvement in hormones

A

some hormones are made of proteins

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5
Q

proteins participate in

A

every cellular activity that helps the body function

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6
Q

protein structure

A

protein is made up of chains of amino acids that are made based on an individual’s DNA

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7
Q

proteins’ structure differ from that of CHO and lipids

A
  • excess dietary protein cannot be stores in the body
  • proteins contain nitrogen, along with carbon, hydrogen, and oxygen
  • some proteins contain sulfur which isn’t found in CHO or lipids
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8
Q

amino acids

A

the building blocks of proteins

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9
Q

how many amino acids are used to make proteins

A

there are 20 amino acids used

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10
Q

types of amino acids used

A

essential and nonessential

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11
Q

how many essential amino acids

A

9

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12
Q

how many nonessential amino acids

A

11

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13
Q

essential amino acids

A

must be consumed in the diet

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14
Q

nonessential amino acids

A

can be synthesized in the body

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15
Q

how are proteins classified

A

by the number of amino acids in the chain

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16
Q

peptides

A

fewer than 50 amino acids

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17
Q

types of peptides

A

dipeptides, tripeptides, and polypeptides

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18
Q

how many amino acid chains do dipeptides have

A

2 amino acids

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19
Q

how many amino acid chains do tripeptides have

A

3 amino acids

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20
Q

how many amino acid chains do polypeptides have

A

3 to 50 amino acids

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21
Q

how many amino acid chains do proteins have

A

more than 50 amino acids (usually from 100-10,000 amino acids linked together)

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22
Q

anatomy of an amino acid

A
  • carbon center
  • amine group (NH2)
  • carboxylic acid group (COOH)
  • hydrogen (H)
  • side chain (R group)
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23
Q

side chain (R group)

A

a unique side chain distinguishes the various amino acids

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24
Q

peptide bonds form through

A

condensation

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25
Q

peptide bonds break through

A

hydrolysis

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26
Q

condensation

A

when the carbon of the acid group (COOH) of one amino acid joins with the nitrogen atom of the amine group (NH2) of a second amino acid and release a molecule of water

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27
Q

hydrolytic reaction

A

when peptide bonds are broken down by hydrolysis, the hydroxyl group (OH) and hydrogen (H) from water are added

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28
Q

hydrolysis

A

a molecule of water is added to the amino acid

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29
Q

conditionally essential amino acids

A

tyrosine and glycine

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30
Q

tyrosine

A

production of neurotransmitters during periods of stress

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31
Q

glycine

A

collagen synthesis during pregnancy

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32
Q

structure impacts

A

function

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33
Q

altering the shape of a protein

A

alters the function of a protein

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34
Q

when the shape of a protein is changed, what aspect of the protein remains unchanged

A

the primary structure is unchanged

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35
Q

4 levels of protein structure

A

primary, secondary, tertiary, and quaternary

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36
Q

primary level of protein structure

A

sequence of amino acids in a polypeptide chain (how they are linked in the chain)

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37
Q

secondary level of protein structure

A

local folding of the chain into alpha helices and beta sheets that depends on the hydrogen bonds (how it folds)

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38
Q

tertiary level of protein structure

A

overall 3D shape of a single polypeptide chain, dependent on the interactions of the side chains (R groups) of each amino acid (how the sequence is set up and how it folds)

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39
Q

quaternary level of protein structure

A

how multiple polypeptide chains assemble into subunits into a single functional protein (larger protein molecule)

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40
Q

denaturation means

A

unfolding

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41
Q

denaturation of proteins occurs in the presence of

A

heat, acids, bases, salts, and mechanical agitations

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42
Q

once a protein is denatured

A

it can’t go back

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43
Q

example of denaturation

A

when cooking an egg, the egg white becomes white with heat (it is becoming denatured) and you cannot revert the egg white back to how it was before the heat

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44
Q

protein digestion begins in the

A

stomach

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45
Q

protein digestion in the stomach

A

gastrin stimulates the release of hydrochloric acid (HCL)

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46
Q

role of HCL in the digestion of proteins

A

HCL denatures the proteins and converts pepsinogen to pepsin

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47
Q

role of pepsin in the digestion of proteins

A

pepsin breaks polypeptides into shorter chains

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48
Q

digestion of proteins continues in the

A

small intestine

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49
Q

polypeptides enter the

A

small intestine

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50
Q

in the small intestine, polypeptides are

A

broken down

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51
Q

role of CCK in the digestion of proteins

A

CCK stimulates the release of proteases by the pancreas

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52
Q

role of proteases in the digestion of proteins

A

proteases break apart polypeptides

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53
Q

types of proteases

A

pepsinogen, trypsin, chymotrypsin, carboxypeptidase, aminopeptidase, dipeptidases, and tripeptidases

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54
Q

pepsinogen is made in the

A

stomach by chief cells

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55
Q

pepsinogen is

A

activated to pepsin by HCL

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56
Q

pepsinogen breaks apart

A

polypeptides into shorter polypeptide chains

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57
Q

trypsin is made in the

A

pancreas

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58
Q

trypsin is released in the

A

small intestine

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59
Q

trypsin breaks apart

A

peptide bonds

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60
Q

chymotrypsin is made in the

A

pancrease

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61
Q

chymotrypsin is released in the

A

small intestine

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62
Q

chymotrypsin breaks apart

A

peptide bonds

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63
Q

carboxypeptidase is made in the

A

pancreas

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64
Q

carboxypeptidase is released in the

A

small intestine

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65
Q

carboxypeptidase breaks free

A

one amino acid at a time from the carboxyl end (COOH) of a peptide chain

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66
Q

aminopeptidase is released in the

A

brush border of the small intestine

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67
Q

aminopeptidase breaks free

A

the end amino acids from tri- and -dipeptides into single amino acids

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68
Q

dipeptidase breaks

A

dipeptides into single amino acids

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69
Q

tripeptidases breaks

A

tripeptides into single amino acids

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70
Q

amino acids are absorbed in the

A

small intestine

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71
Q

from the small intestine, amino acids are transported to

A

the liver

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72
Q

how are amino acids transported from the small intestine to the liver

A

via the portal vein

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73
Q

the most metabolically active organ in the body is

A

the liver

74
Q

in the liver, amino acids are:

A
  • used to synthesize new proteins
  • converted to energy, glucose, and fat
  • released to the bloodstream and transported to cells throughout the body
75
Q

occasionally proteins are absorbed

A

intact

76
Q

amino acids are metabolized in the

A

liver

77
Q

liver metabolizes amino acids depending on

A

the body’s needs

78
Q

most amino acids are (amino acid metabolism)

A

sent into the blood to be picked up and used by cells

79
Q

if the diet is low in CHO (amino acid metabolism)

A

the amino acids are converted into glucose through gluconeogenesis

80
Q

amino acids can be used for energy when (amino acid metabolism)

A

the diet is deficient in kcals (ATP)

81
Q

energy metabolism

A

niacin

82
Q

amino acid pools supply

A

provide a ready supply of amino acids to create proteins on demand for the body’s ongoing need for protein synthesis

83
Q

what does the body do daily that we need amino acid pools

A

the body breaks down and makes proteins daily to maintain tissues and organs

84
Q

extra protein is used to help the body

A

heal

85
Q

protein turnover

A

the process of degrading and synthesizing proteins

86
Q

about how many proteins are turned over daily

A

more than 200 grams of protein is turned over daily

87
Q

transcription

A
  • DNA to mRNA (messenger RNA)
  • copying/the making of the script
88
Q

transcription is the first step in

A

protein synthesis (the making of proteins)

89
Q

transcription happens in the

A

nucleus

90
Q

steps to transcription

A

conversion of genetic information and preparation for translation

91
Q

conversion of genetic information

A

copying a specific gene’s DNA sequence into mRNA

92
Q

the mRNA created serves as a

A

temporary, mobile copy of the genetic information

93
Q

preparation for translation

A

the mRNA molecule carriers the information from the DNA in the nucleus to the cytoplasm

94
Q

where are proteins made

A

the cytoplasm

95
Q

codons

A

sets of 3 nucleotides that specify particular amino acids

96
Q

mRNA includes

A

codons

97
Q

translation

A
  • mRNA to protein
  • building the actual protein
98
Q

translation happens in the

A

cytoplasm

99
Q

three steps of translation

A

reading the mRNA, the amino acid assembly, and the protein formation

100
Q

in the cytoplasm, what reads the mRNA sequence

A

ribosomes

101
Q

each codon in the mRNA corresponds to

A

a specific amino acid

102
Q

amino acid assembly

A
  • tRNA (transfer RNA) molecules bring the appropriate amino acids to the ribosome
  • the ribosome matches the tRNA anticodons to the mRNA codons, linking the amino acids together in the correct order
103
Q

protein formation

A
  • as the ribosome continues to move along the mRNA, it elongates the growing protein chain until it reaches a stop codon
  • at this point, the newly synthesized protein is released
104
Q

sickle cell anemia

A

a common blood disorder that involves abnormal or flawed protein formation

105
Q

deamination

A

the removal of an amine group from an amino acid

106
Q

what is formed from deamination

A

ammonia and a keto acid

107
Q

when the amino acid pool reach capacity

A

amino acids are broken down to be used

108
Q

carbon containing remnants of deamination are:

A
  • converted to glucose (if glucogenic amino acid)
  • converted to fatty acids and stored as TG
  • oxidized for energy via metabolic pathways
109
Q

when we have excess amino acids we

A

pee them out

110
Q

amine group is released in the liver

A

which creates ammonia, which is converted to urea and excreted out in the urine

111
Q

transamination

A

the process of forming nonessential amino acids by transferring the amine group from an essential amino acid to a keto acid to form a nonessential amino acid and a new keto acid

112
Q

functions of proteins

A
  • provide structural support and enable movement
  • act as a catalyst
  • act as a chemical messenger
  • regulate fluid balance
  • help maintain acid base balance
  • contributes to a healthy immune system
  • transport proteins shuttle oxygen, waste products, lipids, some vitamins, sodium, and potassium through the blood and cell membranes
  • provide energy
  • provides satiety
113
Q

proteins act as a catalyst

A

enzymes speed up reactions

114
Q

proteins act as a chemical messenger

A

hormones regulate cell actions

115
Q

proteins regulate fluid balance by

A

a protein marker found in the blood
- albumin
- C-Reactive protein

116
Q

albumin

A

when these levels drop, the body has a hard time keeping fluid where it needs to be

117
Q

edema

A
  • excess fluid
  • albumin level could be low
  • push down on the skin and will take very long to come back up
118
Q

proteins contributes to a healthy immune system

A

antibodies are proteins that bind and neutralize pathogens

119
Q

proteins help transport potassium

A

potassium starts outside the cell but wants to be inside the cell

120
Q

proteins help transport sodium

A

sodium starts inside the cell but wants to be outside the cell

121
Q

proteins provide satiety

A
  • more than any other macronutrient
  • proteins –> carbs –> fats
122
Q

nitrogen balance

A
  • consume enough protein to replace what is used
  • taking in the right amount of nitrogen and not excreting too much
123
Q

positive nitrogen balance

A
  • amount of nitrogen consumed exceeds the amount used
  • associated with periods of growth
  • either need to consume more or the body doesn’t excrete a lot out
  • pregnancy, childhood/adolescence, exercise
124
Q

negative nitrogen balance

A
  • the amount of nitrogen used exceeds the amount consumed
  • illness, injury, inadequate protein intake, malnutrition, stress
125
Q

RDA for protein

A

0.8 g/kg for adults >18

126
Q

how to find the RDA for protein

A

divide your weight from pounds into kg then multiple by 0.8

127
Q

AMDR for protein

A

10-35% of total kcals

128
Q

protein intake recommendations for people over 65

A

1 g/kg (have to think about maintaining bone density)

129
Q

protein intake for athletes

A

athletes can need 50-100% more protein, typically recommendations don’t exceed 2.2 g/kg

130
Q

protein sources

A

high quality protein, complementary and complete protein

131
Q

high quality protein

A
  • digestible
  • contains all essential amino acids
  • adequate protein to synthesize nonessential amino acids
132
Q

complete proteins

A
  • contain all 9 essential amino acids
  • usually animal sources (meat, fish, poultry, dairy)
  • exception: soy protein and quinoa
133
Q

incomplete proteins

A
  • low in one or more essential amino acids
  • the limiting amino acid (missing some parts)
134
Q

examples of incomplete proteins

A

grains, nuts, seeds, legumes

135
Q

complementary proteins

A
  • combining incomplete proteins with a food that supplies the limiting amino acid
136
Q

examples of complementary proteins

A
  • rice + beans = a full protein
  • legumes + grains or nuts or seeds = a full protein
137
Q

food sources of protein

A

eggs, meat, fish, poultry, soy, and dairy

138
Q

a 3 oz serving of cooked meat, fish, or poultry

A
  • provides about 7g of protein per oz
  • 3 oz serving gives you about 21g of protein
  • about the size of a deck of cards
139
Q

best approach for sources of protein

A

eat a variety of foods

140
Q

protein supplements are typically unnecessary because

A

most Americans well exceed their protein needs

141
Q

too much protein

A
  • may increase risk for cardiovascular disease
  • increased risk for osteoporosis
  • increased risk for kidney stones
142
Q

may increase risk for cardiovascular disease

A

high protein can be associated with high saturated fats

143
Q

increased risk for osteoporosis

A
  • if there is low calcium intake
  • high protein with adequate calcium intake is protective of the bone
144
Q

increased risk for kidney stones

A

diet high in animal protein and low in CHO lowers urine pH, increasing risk for kidney stones

145
Q

an overemphasis on protein can result in

A

a displacement of other key nutrients from fruits, vegetables, and whole grains

146
Q

too little protein

A
  • increase risk for osteoporosis
  • malnutrition
  • inadequate protein
147
Q

malnutrition

A

protein energy malnutrition (PEM)

148
Q

inadequate protein

A
  • cell lining of GI tract not sufficiently replaced
  • digestive function is inhibited
  • absorption of food is reduced
  • immune system is compromised
149
Q

protein energy malnutrition (PEM)

A
  • protein is used for energy rather than its functions in the body (we don’t want to use protein for energy!!)
  • more prevalent in infants/children
  • in the US, elderly people are more at risk
150
Q

malnutrition (PEM)

A
  • 1 in 8 people don’t have adequate protein intake, kcal, or both
  • available protein is then used as an energy source
  • lack of protein damages the GI tract
  • decreased immune function
151
Q

types of PEM

A

kwashiorkor and marasmus

152
Q

kwashiorkor

A
  • severe protein deficiency
  • have enough energy and fat but not enough protein
  • can come on very quickly (less than a month)
  • no visible bones, fuller cheeks, very bloated stomach
153
Q

symptoms of kwashiorkor

A
  • edema in the legs, feet, and hands (albumin drops)
  • diminished muscle tone and strength
  • brittle hair that is easy to pull out
  • pale, sad, apathetic appearance
  • prone to infection, increased HR, fluid in lungs, pneumonia, septicemia, and electrolyte imbalances
154
Q

marasmus

A
  • chronic starvation
  • severe malnutrition in all the nutrients
  • very squared off shoulders (sign of low fat consumption)
  • temporal areas and under eyes sunken in (missing the pad of fat)
  • results from severe deficiency in kcals
155
Q

marasmus symptoms

A
  • frail, emancipated appearance
  • weakened and appear apathetic
  • often cannot stand without support
  • appears older in age
  • hair is thin, dry, and lacks sheen
  • low body temperature and BP
  • prone to dehydration, infections, and unnecessary blood clotting
156
Q

treatment for PEM

A
  • medical and nutritional treatment can reduce mortality rate
  • should be implemented carefully and slowly
157
Q

step 1 in treatment for PEM

A

address life threatening factors

158
Q

addressing life threatening factors first

A
  • severe dehydration
  • fluid and nutrient imbalance
159
Q

step 2 in treatment for PEM

A

restore depleted tissue

160
Q

restoring depleted tissue second

A

gradually provide nutritionally dense kcals and high quality protein

161
Q

step 3 in treatment for PEM

A

transition to foods and introduce physical activity

162
Q

transitioning to foods and introducing physical activity third

A

any type of movement

163
Q

why people choose a vegetarian diet

A

for a number of reasons
- ethical
- religious
- environmental
- health

164
Q

lacto-vegetarian eats

A

grains, veggies, fruits, legumes, seeds, nuts, and dairy

165
Q

lacto-vegetarian avoids

A

meat, fish, poultry, and eggs

166
Q

lacto-ovo-vegetarian eats

A

grains, veggies, fruits, legumes, seeds, nuts, dairy, and eggs

167
Q

lacto-ovo-vegetarian avoids

A

meat, fish, and poultry

168
Q

ovo-vegetarian eats

A

grains, veggies, fruits, legumes, seeds, nuts, and eggs

169
Q

ovo-vegetarian avoids

A

meat, fish, poultry, and dairy

170
Q

vegan eats

A

grains, veggies, fruits, legumes, seeds, and nuts

171
Q

vegan avoids

A

any animal foods (meat, fish, poultry, dairy, and eggs)

172
Q

pescetarian eats

A

grains, veggies, fruits, legumes, seeds, nuts, dairy, eggs, and fish

173
Q

pescetarian avoids

A

meat and poultry

174
Q

semi vegetarian eats

A

a vegetarian diet that occasionally includes meat, fish, and poultry

175
Q

semi vegetarian avoids

A

meat, fish, and poultry on occasion

176
Q

potential benefits of a vegetarian diet

A

reduced risk of: cardiovascular disease, hypertension, diabetes, cancer, stroke, and obesity

177
Q

with a vegetarian diet, at risk of deficiencies in

A
  • protein
  • calcium
  • iron
  • B12
  • zinc
  • vitamin A
  • vitamin D
  • omega 3 fatty acids
178
Q

iron for women

A

women need 18 mg a day

179
Q

iron for men

A

men need 8 mg a day

180
Q

B12

A

have to be really cautious when pregnant

181
Q

zinc

A
  • comes in a lot of animal products
  • aid in the immune system

Nutrition Exam 2 (5 decks)

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