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NASM CN > Protein > Flashcards

Protein Flashcards

1
Q

Acid–Base Balance

A

The process of achieving, or the state of, equilibrium between acidic and alkaline molecules.

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2
Q

Amino Acids

A

The organic building blocks of proteins containing both a carboxyl and an amino group.

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3
Q

second-most abundant molecule in fat-free bodily tissues

A

protein

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4
Q

role of protein

A

acid–base balance, energy production, cell signaling, and nutrient transport

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5
Q

what elements form the amino acids?

A

carbon (C), hydrogen (H), oxygen (O), and nitrogen (N)

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6
Q

how many amino acids are needed in the body?

A

20

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7
Q

five components of amino acid structure

A

a central carbon, a carboxyl group (organic acid – COOH), a hydrogen, an amino group (NH2), and a side chain (R group).

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8
Q

Essential Amino Acid (EAA)

A

Amino acids that are necessary for bodily functions but cannot be synthesized by the body and, therefore, must be obtained in the diet.

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9
Q

Branched Chain Amino Acid

A

The three essential amino acids (leucine, isoleucine, and valine) which are abundant in skeletal muscle tissue and named for their branch-like structure.

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10
Q

Conditionally Essential Amino Acids

A

Amino acids that are not typically essential, but can become essential during times of extreme dietary insufficiency, illness, or trauma.

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11
Q

nonessential amino acids list

A

Alanine

Asparagine

Aspartic acid

Glutamic acid

Serine

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12
Q

conditionally essential amino acids list

A

Arginine

Cysteine

Glutamine

Glycine

Proline

Tyrosine

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13
Q

essential amino acids list

A

Histidine

Lysine

Methionine

Phenylalanine

Threonine

Tryptophan

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14
Q

branch chain amino acid list

A

Isoleucine

Leucine

Valine

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15
Q

Gluconeogenesis

A

A metabolic pathway that results in the generation of glucose from non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.

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16
Q

Glucogenic amino acids

A

amino acids that can have their carbon backbone converted to glucose by the process of gluconeogenesis, or they can be converted to an intermediate compound that may enter the Krebs cycle directly

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17
Q

Ketogenic amino acids

A

amino acids that may become acetoacetate (a ketone body) or acetyl-CoA prior to entering the Krebs cycle for the generation of ATP.

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18
Q

Glucogenic amino acid list

A

Alanine

Asparagine

Aspartic acid

Cysteine

Valine

Glutamic acid

Glutamine

Glycine

Proline

Serine

Arginine

Histidine

Methionine

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19
Q

how many glucogenic amino acids are there?

A

13

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20
Q

ketogenic amino acid list

A

Leucine

Lysine

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21
Q

how many ketogenic amino acids are there?

A

2

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22
Q

Glucogenic or Ketogenic amino acid list

A

Tyrosine

Isoleucine

Tryptophan

Phenylalanine

Threonine

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23
Q

Protein Synthesis

A

Process of joining amino acids with peptide bonds to form proteins.

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24
Q

Dehydration Synthesis

A

The joining of two large molecules by removing one hydrogen from one molecule and a hydroxyl group (OH) from another molecule and then binding the two larger molecules together on the newly freed bonds.

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25
Q

How are nonessential amino acids made?

A

They’re made by breaking other amino acid or nitrogen-containing compounds apart, and then reusing the components.

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26
Q

In order to make tyrosine, you need to eat enough ______

A

Phenylalanine

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27
Q

Can your body store amino acids?

A

No

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28
Q

Proteins are part of every bodily fluid except……

A

Bile and urine

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29
Q

Plant sources of complete protein

A

Quinoa and soy

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30
Q

_______ and ________ help muscles contract to make your body move

A

Actin and myosin

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31
Q

What amino acid helps keep blood vessels open?

A

L-arginine

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32
Q

What amino acid is part of epinephrine and norepinephrine?

A

Tyrosine

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33
Q

What amino acid is needed for serotonin?

A

Tryptophan

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34
Q

______ is a protein that helps transport oxygen in blood to body cells

A

Hemoglobin

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35
Q

Kwashiorkor

A

A form of protein deficiency that results in muscle loss, failure to grow, lower immunity, increased risk for disease, and weakened respiratory and cardiovascular systems

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36
Q

Marasmus

A

A type of severe protein energy malnutrition that causes a debilitating amount of muscle loss and often death

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37
Q

What does the body do with excess protein?

A

It breaks down and converts into body fat or glycogen for energy storage. It’s nitrogen containing components are removed and excreted through urine by the kidneys

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38
Q

Which amino acids are more limited in plant foods?

A

Cysteine
Lysine
Methionine
Tryptophan

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39
Q

Beans are high in _______ but low in ________ and _________

A

Lysine, cysteine and methionine

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40
Q

Nuts, seeds and grains are high in ______ and ________ but limited in _________

A

Menthionine and cysteine, lysine

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41
Q

Rice is high in _________ but limited in _______

A

Methionine, lysine

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42
Q

Corn is high in _________ but is low in ______ and _______

A

Methionine, lysine and tryptophan

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43
Q

On labels, high protein =

A

10 g or more per serving

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44
Q

On labels, good source of protein =

A

5 to 9.9 g per serving

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45
Q

On a label, more/extra/plus protein =

A

At least 5 g *more per serving

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46
Q

On a label, fortified/enriched with protein =

A

At least 5g *more per serving

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47
Q

Sarcopenia

A

The progressive decline in muscle mass and strength that happens naturally with aging

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48
Q

50% of bone volume is ….

A

Protein

49
Q

Soys’s two main isoflavones- _________ and _______, have weak estrogen like effects

A

Genistein and daidzein

50
Q

Dehydration Synthesis

A

The joining of two large molecules by removing one hydrogen from one molecule and a hydroxyl group (OH) from another molecule and then binding the two larger molecules together on the newly freed bonds.

51
Q

Peptide Bond

A

The bond between two amino acids, occurring between the carboxyl group of one and the amino group of the other.

52
Q

Hydrolysis

A

Breakdown of one large molecule into two smaller molecules via the donation of one hydrogen and one hydroxyl group from water to the smaller molecules, respectively.

53
Q

When proteins are consumed, they must first be broken down into ___________________by digestion to be absorbed in the ______________.

A

amino acids, intestines

54
Q

after protein is absorbed, it can be transported to ________________ tissues and recombined to form new proteins such as ___________, __________, and ______________.

A

peripheral
collagen, myosin, hemoglobin

55
Q

Bodily proteins are most often formed by at least _______ amino acids.

A

50

56
Q

Oligopeptide

A

A chain of four to nine amino acids.

57
Q

Polypeptide

A

A chain of 10 or more amino acids.

58
Q

The three major muscle proteins are:

A

myosin, actin, titin

59
Q

titin has about __________ amino acids

A

30,000 amino acids

60
Q

myosin has about ________ amino acids

A

6,000 amino acids

61
Q

actin has about ______ amino acids

A

400 amino acids

62
Q

___________uses energy from ATP to grab ________ and flex in unison with many other myosin proteins to produce a muscle contraction.

A

myosin, actin

63
Q

function of titin

A

helps provide a muscle’s elasticity so it can return to its resting length following muscle contractions.

64
Q

which protein stretches over the entire muscle cell?

A

titin

65
Q

Gastrin

A

A hormone released when food is ingested to stimulate release of digestive fluids.

66
Q

Pepsinogen

A

A proenzyme secreted by the stomach as a precursor to pepsin.

67
Q

Pepsin

A

An enzyme in the stomach that begins breaking peptide bonds.

68
Q

Duodenum

A

It is the first section of the small intestine where some digestion occurs, and it is located immediately after the stomach and leads into the jejunum.

69
Q

Secretin

A

A hormone that stimulates the liver and pancreas to produce bile and bicarbonate; inhibits gastrin release.

70
Q

Cholecystokinin

A

A hormone secreted by the duodenum that causes release of enzymes and bile.

71
Q

Protease Enzymes

A

Enzymes in the small intestine that break long peptide chains into shorter peptide chains.

72
Q

Peptidase

A

An enzyme that breaks down small peptides.

73
Q

Aminopeptidases

A

Enzymes that cleave individual amino acids from a peptide chain so they may be absorbed.

74
Q

Hepatic Portal Vein

A

The vein that transports blood from the spleen, stomach, pancreas, and the intestinal tract to the liver.

75
Q

Collagen

A

A protein formed of a triple-helix structure with great tensile strength, found primarily in skin, muscles/connective tissue, and bones.

76
Q

tensile strength

A

Ability of a material to resist breaking under tension.

77
Q

Elastin

A

A protein with high elasticity, found mainly in the skin.

78
Q

Keratin

A

A protein found in hair and nails.

79
Q

Sodium–Potassium Pump

A

A protein found on the cell membrane that transports sodium and potassium to create electrochemical gradients across the membrane.

80
Q

Albumin

A

A protein found in the blood stream that helps draw water into the blood vessel from surrounding tissue.

81
Q

Hemoglobin

A

An iron-containing protein found on red blood cells, binds oxygen and other molecules for transport in the blood.

82
Q

protein need for no activity

A

0.8 to 1.2 g/kg body weight

83
Q

protein need for light to moderate cardiovascular activity

A

1.2 to 1.6 g/kg body weight

84
Q

protein need for Light to Moderate resistance training

A

1.5 to 2.0 g/kg body weight

85
Q

protein need for Moderate to Vigerous cardiovascular activity

A

1.5 to 2.0 g/kg body weight

86
Q

protein need for Moderate to Vigerous resistance training

A

1.7 to 2.2 g/kg body weight

87
Q

what is NH2?

A

the amino group

88
Q

what is the organic acid of a carboxyl group?

A

COOH

89
Q

What is the byproduct of dehydration synthesis?

A

water

90
Q

what are the reactants in dehydration synthesis?

A

hydrogen from one amino acid and a hydroxyl group (OH) from a second amino acid

91
Q

what bond joins the amino acid and the hydroxyl group in a dehydration synthesis?

A

peptide bond

92
Q

what causes denaturation?

A

temperature, pH, and enzymes, cooking

93
Q

Unlike with carbohydrates and fats, enzymes for protein in the __________ are relatively inactive and do little to aid in digestion.

A

saliva

94
Q

chewing food causes the stomach wall to release _________ in anticipation of the digestion process

A

gastrin

95
Q

gastrin causes the release of ____________________ and the hormone _____________ in the stomach.

A

hydrochloric acid and pepsinogen

96
Q

When pepsinogen contacts the hydrochloric acid, it releases the active enzyme _________

A

pepsin

97
Q

______________ acid denatures the protein and _______ begins breaking the very long polypeptide chains into smaller peptide chains (hydrolysis reaction).

A

hydrochloric acid, pepsin

98
Q

the breaking of polypeptide chains into smaller peptide chains due to pepsin

A

hydrolysis reaction

99
Q

As the food passes from the stomach into the duodenum of the small intestine, the intestinal cells release the hormones _______ and _____________

A

secretin, cholecystokinin

100
Q

function of secretin

A

acts as a regulator of digestion, reducing acid release to help restore pH when eating ceases

101
Q

Cholecystokinin causes the pancreas to release what enzymes into the small intestine?

A

the protease enzymes trypsin, chymotrypsin, carboxypeptidase, and elastase

102
Q

which enzymes break peptides into single amino acids?

A

peptidases and aminopeptidases

103
Q

what carries amino acids and dipeptides to the liver?

A

the hepatic portal vein

104
Q

what percent of plant protein can be absorbed?

A

85%

105
Q

what percent of animal protein can be absorbed?

A

95%

106
Q

what amino acids form collagen?

A

glycine, proline, and hydroxyproline

107
Q

collagen has a ____________ structure

A

triple helix

108
Q

protein RDA for women

A

46 g

109
Q

protein RDA for men

A

56 g

110
Q

protein needs for no activity

A

0.8 to 1.2 g/kg body weight

111
Q

protein needs for light/mid cardiovascular exercise

A

1.2 to 1.6 g/kg body weight

112
Q

protein needs for light/mid resistance exercise

A

1.5 to 2.0 g/kg body weight

113
Q

protein needs for mid-hard cardio

A

1.5 to 2.0 g/kg

114
Q

protein needs for mid-hard resistance

A

1.7 to 2.2

115
Q

Maintaining as much muscle mass as possible while dieting can be achieved with at least ______________ grams per kilogram of protein and regular resistance training

A

1.8 to 2.2 grams per kilogram

116
Q

individuals 65 years of age and older consume at least _____ to ______ grams of protein per kilogram bodyweight

A

0.9 to 1.6

117
Q

24-hour net muscle protein synthesis may be optimal if stimulated with dietary protein (containing leucine) every _______ hours

A

3 hours

118
Q

Post-workout protein consumption with carbohydrates in a ______ or ______ ratio of carbohydrates to protein can accelerate the replenishment of muscle glycogen

A

3:1 or 4:1

119
Q

PVT stands for

A

phenylalanine, valine,

NASM CN (14 decks)

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