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Protein Flashcards

1
Q

Composed of C, H, O, N, and sometimes S

A

Protein

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2
Q

Only nutrient that can make new cells and rebuild tissue.

A

Protein

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3
Q

Basic material of every body cell.

A

Protein

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4
Q

Composed of amino acids linked by peptide bonds.

A

Protein

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5
Q

Greek word that means “holding first place” and term coined by Mulder (Dutch Scientist) in 1840.

A

Protein

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6
Q

Molecule w/ a central carbon to which an amino group, a carboxyl group and a functional group are attached.

A

Amino acid

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7
Q

How many amino acid are needed by the human body?

A

20

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8
Q

How many from the 20 AA are considered essential, which must be supplied by the diet?

A

10

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9
Q

General structure of AA

A

central carbon, amino group, a carboxyl group and a functional group

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10
Q

AA classification

A

Functional groups, Pathway of catabolism, essentiality

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11
Q

Functional groups

A

Basic, acidic, neutral

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12
Q

Basic Functional group AA

A

lysine, arginine, histidine

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13
Q

acidic Functional group AA

A

aspartic acid, glutamic acid

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14
Q

neutral Functional group AA

A

glycine, serine, threonine, etc

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15
Q

2 pathway of catabolism

A

glucogenic, ketogenic

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16
Q

AA that can be catabolized to produce glucose (gluconeogenesis)

A

glucogenic

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17
Q

AA that can be catabolized to produce acetyl-CoA (-> ketone bodies) and ipids

A

ketogenic

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18
Q

3 classifications of Essentiality of AA

A

essential, nonessential, conditionally essential

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19
Q

Indespensable AA

A

Essential

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20
Q

Dispensable

A

Nonessential

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21
Q

Indispensable at certain life stages

A

Conditionally essential

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22
Q

Essential AA

A

(PVTTIMHALL) Phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, histidine, arginine, leucine, lysine

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23
Q

Conditionally essential

A

Proline, serine, tyrosine, cysteine, taurine, glycine

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24
Q

Nonessential

A

Glutamate, alanine, aspartate, glutamine

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25
Q

Protein classification

A

structure, shape, composition

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26
Q

4 levels of protein structure

A

primary structure, secondary structure, tertiary structure, quaternary structure

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27
Q

Classification of protein by shapes

A

fibrous, globular, membrane

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28
Q

Proteins which are long coiled or folded chains of AA bound in parallel line and insoluble in water and dilute salt solutions; serve in structural roles

A

Fibrous

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29
Q

Protein which are coiled, tightly wound structure & roughly spherical; relatively water soluble; constitute most of the soluble proteins in the cell

A

Globular

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30
Q

Proteins associated with various membrane systems; insoluble in aqueous solutions; more hydrophobic AA

A

Membrane

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31
Q

Example of Fibrous protein

A

keratin

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32
Q

Example of globular protein

A

hemoglobin

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33
Q

Example of membrane protein

A

phospholipid membrane

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34
Q

Protein classification by composition

A

simple, conjugated, derived

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35
Q

Protein which are primary components are AA

A

simple

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36
Q

Proteins which are composed of AA and other components

A

conjugated

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37
Q

Proteins which are products of partial hydrolysis

A

derived

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38
Q

Examples of simple proteins

A

albumin (egg white), globulins (egg yolk), glutenins or glutelins (wheat, rice), prolamines (wheat, corn) scleroproteins (bones, connective tissues)

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39
Q

protein source with amino acid score: 100%

A

animal origin

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40
Q

Biological functions of protein

A

Enzymes - to accelerate rates of biological reactions
Regulation of body processes - to assist in the ability of other proteins to carry out their functions (hormones)
Storage - to provide reservoir like hemoglobin
contraction and motility - for muscles
structure - to provide strength like collagen and keratin
protection - to enhance immunity like immunoglobulins

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41
Q

amino acid score of animal origin

A

100%

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42
Q

Examples of conjugated proteins

A

glycoproteins, lipoproteins, nucleoproteins, phosphoproteins, metalloproteins, hemoproteins, flavoproteins, mucoproteins

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43
Q

General functions of protein

A
  1. body building or structural
  2. essential for growth
  3. source of energy (secondary)
  4. regulator of body processes
  5. transport of certain substances
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44
Q

Examples of derived proteins

A

Primary - edestan, myosan, metaproteins, coagulated proteins
Secondary - proteoses, peptones, and peptides

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45
Q

protein source with true digestibility: 95-98%

A

animal origin

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46
Q

true digestibility of animal origin

A

95-98%

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47
Q

protein source which concentrations increase after cooking

A

animal origin

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48
Q

protein source which includes pulses, cereal & cereal products

A

plant origin

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49
Q

protein source with amino acid present, could be 1 or more limiting amino acids

A

plant origin

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50
Q

plant origin examples

A

pulses, cereal & cereal products

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51
Q

how many limiting amino acid present in a plant origin?

A

one or more limiting amino acids

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52
Q

protein source with true digestibility in natural foods: 70-85%

A

plant origin

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53
Q

true digestibility of plant origin

A

70-85%

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54
Q

bioavailability of protein in pulses

A

20-25%

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55
Q

bioavailability of protein in flour

A

7-12%

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56
Q

meat alternative made from soy protein and other ingredients to simulate various kinds of meat

A

meat analogues

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57
Q

textured vegetable protein (TVP) and tofu

A

meat analogues examples

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58
Q

Capacity of food proteins to provide nitrogen and essential AA for human growth and functions

A

Protein quality
- checks AA content & efficiency of digestion
- lower protein quality means more intake of protein

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59
Q

What highlights nitrogen balance

A

Protein quality

60
Q

reflects the equilibrium between protein intake and losses

A

nitrogen balance

61
Q

Nitrogen balance

A

equilibrium: intake = output
positive nitrogen balance: intake > output (children, pregnant, convalescing person/recovering)
negative nitrogen balance - intake < output (underwent surgery, fever, immobility, shock, burns)

62
Q

Factors affecting protein utilization

A
  1. AA balance
  2. emotional stress
  3. caloric intake
  4. inborn errors of metabolism
  5. food processing
63
Q

How to determine protein quality

A
  1. biological value
  2. amino scoring
  3. protein digestibility
  4. protein conc.
  5. protein/energy ratio
64
Q

refers to percentage of nitrogen absorbed from the dietary protein actually used by the body

A

biological value
-higher BV -> higher N retained; means the food is supplying essential AA

65
Q

Formula of biological value

A

BV = (N retained) / (N absorbed) = ((Dietary N - (Urinary N - Fecal N)) / Dietary N - Fecal N) x 100

66
Q

BV of some foods

A

Egg: 100
Milk: 93
Rice: 86
Fish, beef: 75
Corn: 72
Peanut flour: 56
Wheat gluten: 44

67
Q

Calculation of the proportion of each EAA in protein or diet relative to reference protein

A

AA Scoring

68
Q

Value of the limiting AA with the lowest score in a protein

A

AA score (chemical score)

69
Q

Formula of AA score

A

AA score = (mg of EAA in 1g of food protein) / (mg of EAA in 1g of reference protein)

70
Q

Measure of the amount of protein available for absorption after digestion that is dependent on the shape (fibrous or globular), presence of dietary factors, and heat treatment

A

Protein digestibility

71
Q

A variation of protein digestibility that has been developed

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

72
Q

provides adequate amounts of essential amino acids to adequately support human protein synthesis

A

plant combination

73
Q

official assay for evaluating protein quality in human nutrition

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

74
Q

complementary proteins of Kanin + Munggo Guisado

A

High Met (rice) + Low Met (beans)

75
Q

Chemical score of limiting AA multiplied by its true digestibility

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

76
Q

Complementary proteins of mais con yelo

A

High Lys (milk) + Low Lys (corn)

77
Q

PDCAAS Formula

A

PDCAAS = ((mg of 1st limiting AA in 1g test protein) / (mg of the same AA in 1g reference protein)) x TD (%) x 100

TD is true fecal digestibility of the test protein

78
Q

excellent protein combinations of grains and legumes

A

-rice + beans
-pea soup + toast
-lentil curry +rice

79
Q

to rate the overall quality of protein based on the amount of essential AA contained

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

80
Q

excellent protein combinations of grains and dairy

A

-pasta + cheese
-rice pudding
-cheese sandwich

81
Q

Based on the AA that is in the shortest supply when compared to the reference (scoring) protein

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

82
Q

This scoring pattern is based on the IAA requirements of preschool-age children

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

83
Q

excellent protein combinations of legumes and seeds

A

-garbanzo beans + sesame seeds
-hummus (dip or soup)

84
Q

Digestibility of protein is factored into the score by way of fecal digestibility

A

Protein Digestibility Corrected Amino Acid Score (PDCAAS)

85
Q

addition of protein rich food to a regular diet to increase protein content and quality

A

protein supplementation

86
Q

PDCAAS Example

A

common digestibility percentages include 98% for egg protein; 95% for casein, soy and collagen; 91% for wheat protein

87
Q

increase protein content and quality

A

addition of protein rich food to a regular diet

88
Q

How to interpret PDCAAS

A

If a protein is completely missing just one essential AA, the PDCAAS is 0.
If a protein with a low amount of one essential AA ha a PDCAAS of 20, then the protein provides only 20% of that particular AA when compared to the scoring pattern.
Thus, only 20% of this protein is possible available for protein synthesis in the human body.

89
Q

example of protein supplementation

A

-Tuna spread + cheese = Tuna Melt Sandwich

-Pasta + Ground Beef + Cheese/Cream = Lasagna

90
Q

Protein concentration (density)

A

—-table—-

91
Q

-Tuna spread + cheese = Tuna Melt Sandwich

-Pasta + Ground Beef + Cheese/Cream = Lasagna

A

example of protein supplementation

92
Q

To describe whether a diet provides adequate amounts of protein
- indicates the amount of protein that the diet provides relative to energy

A

Protein/Energy Ratio (net dietary protein calories present)

93
Q

protein turnover is composed of

A

SYNTHESIS where amino acids are joined to form peptides and protein AND DEGRADATION which results in amino acids that are recycled

94
Q

Formula of protein/energy ratio

A

((metabolizable energy from dietary protein) / (metabolizable energy in diet)) x 100

95
Q

Formula on %protein calories

A

(protein calories/total kcal intake) x 100

96
Q

amino acids are joined together to form peptides and protein

A

Synthesis in protein turnover

97
Q

meat analogues examples

A

textured vegetable protein (TVP) and tofu

98
Q

amino acids are recycled

A

Degradation in protein turnover

99
Q

Fusarium graminearum

A

a mycoprotein example of meat analogue

100
Q

dependent on the simultaneous presence of all the amino acids for the specific protein & energy

A

Protein synthesis

102
Q

substances/structures that require protein synthesis

A

cells, glands, muscles, organs, fluid and secretions

103
Q

a mycoprotein example of meat analogue

A

Fusarium graminearum

104
Q

metabolic events in Cell Nucleus

106
Q

Site of synthesis for these metabolic events:

-DNA serves as templet for mRNA
-mRNA copies DNA code
-mRNA leaves the nucleus

A

Cell nucleus

107
Q

meat analogue has _____ digestibility

108
Q

metabolic events in Ribosomes in the Cytoplasm

A

-mRNA attach to ribosome to specify sequence of amino acid

-tRNA collect amino acids from cell fluid and brings these to mRNA which specifies amino acid sequence

-ribosome moves along mRNA as each amino acid is brought by tRNA

-completed protein is released from ribosome and mRNA is degraded

110
Q

proteins which contain all essential amino acids in amounts sufficient for growth & maintenance

A

complete or high biological (HBV) proteins

111
Q

Site of synthesis for these metabolic events:

-mRNA attach to ribosome to specify sequence of amino acid

-tRNA collect amino acids from cell fluid and brings these to mRNA which specifies amino acid sequence

-ribosome moves along mRNA as each amino acid is brought by tRNA

-completed protein is released from ribosome and mRNA is degraded

A

Ribosomes in cytoplasm

113
Q

site of protein synthesis which consists of RNA and protein

114
Q

all animal origin foods except gelatin

A

complete or high biological (HBV) proteins

115
Q

proteins which maintain life but do not support growth

A

partially complete proteins

116
Q

What are the genera principles of protein metabolism?

A

-amino acid are in dynamic state
-proteins must be supplied to the body on a daily basis
-synthesis of proteins is controlled by DNA
-synthesis of proteins follow the all or none law
-protein utilization is closely interrelated w/ fat & carbohydrate metabolism
-amino acids can be recycled

117
Q

gliadin (wheat) and legumin (legumes)

A

partially complete proteins

118
Q

amino acids are in a _______ state

119
Q

proteins which cannot support life or growth

A

incomplete proteins

120
Q

zein (corn), gealtin, and most plant proteins

A

incomplete proteins

121
Q

synthesis of proteins follow the ______ or _______ law

122
Q

plant combination which provides adequate amounts of essential amino acids to adequately support human protein synthesis

A

protein complementary

123
Q

synthesis of protein is controlled by

124
Q

Proteins must be supplied to the body on a ______ basis

125
Q

protein utilization is closely interrelated with _______ & _______ metabolism

A

fat, carbohydrate

126
Q

__________ can be recycled

A

amino acids

127
Q

results in amino acids that join the amino acid pool

A

Protein degradation

128
Q

process of protein degradation

A

protein -> peptide -> amino acids;

nitrogen - incorporated in niacin & creatinine

129
Q

proteins (ex. proline, glitamate, serine, and threonine) degrade at different rates based on

A

physiological status and amino acid composition

130
Q

fates of amino acids not used for synthesis

A

-DEAMINATION (transamination, oxidative deamination, deamination by amino acid oxidase)

-CARBON SKELETONS (oxidized, synthesis of glucose or fatty acids)

131
Q

transamination, oxidative deamination, deamination by amino acid oxidase

A

DEAMINATION

132
Q

oxidized, synthesis of glucose or fatty acids

A

CARBON SKELETONS

133
Q

What are the protein (CHON) requirements (g/kg DBW) for each age group?

A

Infants - 2.75 to 3.00
Children - 1.50 to 2.00
Early Adolescents - 1.50
Older Adolescents - 1.25
Adults - 1.12

134
Q

Protein which is 10-15% of TEA is affected by what factors?

A
  1. Body size
  2. Growth
  3. Pregnancy and Lactation
  4. Aging
135
Q

state of deficit in body protein or in or more of the essential amino acids

A

protein deficiency

136
Q

signs of protein deficiency

A

wasting of tissue, weight loss, general weakness and malaise, reduced resistance to infection, dry and scaly skin, delayed wound healing, nutritional edema, hypoproteinemia, and pallor (anemia)

137
Q

results from inadequate dietary protein, energy or both

A

protein energy malnutrition

138
Q

protein energy malnutrition common in 1-3 years of age can cause

A

mortality, morbidity, and impairment of physical and mental growth

139
Q

types of prolonged protein energy malnutrition

A
  1. Kwashiorkor
  2. Marasmus
140
Q

disease occurs when the next baby is born, inadequate protein intake with fair or normal intake of energy , occurs during weaning stage where foods which lacks amino acids are given to child

A

Kwashiorkor

141
Q

results from deficiency of both protein and energy (predominantly energy deficiency)

142
Q

characteristics of marasmus

A

wasting, emaciation, no edema, quiet, apathetic

143
Q

not toxic but taxing to liver, kidneys, and circulatory system

A

excess protein

144
Q

infants -> increase in ____ and _____ (not to exceed: ___ g/kg/day)

A

BUN, creatinine, 3

145
Q

excess protein with adequate CHO and fat lead to

A

adiposity or obesity

FN 131 lec (12 decks)

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