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Biochemistry 1 > Amino acids and Proteins > Flashcards

Amino acids and Proteins Flashcards

1
Q

what is the most abundant macro-nutrient in the body?

A

PROTEIN

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2
Q

what are the functions of proteins in the body?

A 
signaling
structure
immunity
transport
enzymes
fluid balance
buffers
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3
Q

what is the chemical messenger made in 1 part of the body regulates another part?

A

hormones

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4
Q

what is the hormone made of multiple amino acids?

A

peptide hormones

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5
Q

thyroid hormones (thyroxine) and catecholamines are derived from which amino acids?

A

Tyrosine

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6
Q

tyrosine gives rise to what Amino Acid Derivatives?

A 
thyroid hormones (thyroxine)
catecholamines
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7
Q

what are catecholamines?

A

Neurotransmitters in brain

  • dopamine
  • epinephrine
  • norepinephrine
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8
Q

Histidine gives rise to what Amino Acid derivatives?

A

Histamine

immune repsonse, associated with allergies

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9
Q

what is histamine’s functions?

A

immune response, associated with allergies

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10
Q

tryptophan gives rise to what Amino Acid derivatives?

A

Serotonin, Niacin, and melatonin

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11
Q

what are the functions of serotonin?

A

Neurotransmitter regulating mood, sleep, and appetite

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12
Q

what are the functions of melatonin?

A

regulates sleep-wake cycle

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13
Q

what are the small protiens that act as regulators of growth and differentiation?

A

Cytokines

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14
Q

Interleukin-1 (IL-1), Tumor Necrosis Factor (TNF-Alpha), Interleukin-6 (IL-6), Interleukin-10 (IL-10), and C-Reactive Proteins (CRP) are examples of what?

A

Cytokines

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15
Q

what are some examples of cytokines?

A 
Interleukin-1
Interleukin-6
Interleukin-10
Tumor Necrosis Factor
C-Reactive Proteins
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16
Q

when are cytokines produced?

A

they are produced during acute and chronic inflammation, cancer, obesity, stress, injury and degenerative disc disease

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17
Q

what is the Cytokine that is the best indicator of Inflammation?

A

C-Reactive Protein

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18
Q

what is the Cytokine that breaks down adipose tissue?

A

Interleukin-6

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19
Q

when is the Cytokine interleukin-10 produced?

A

produced during exercise

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20
Q

what is the Function of the Cytokine C-Reactive Protein?

A

it is the best indicator of inflammation

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21
Q

what is the Cytokine that is produced during exercise?

A

Interleukin-10

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22
Q

what is the function of Interleukin-6?

A

it breaks down adipose tissue

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23
Q

Some of the biological functions of proteins are structural. what are the two structural proteins?

A

Fibrous Proteins

Contractile Proteins

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24
Q

Collagen, elastin, and keratin are examples of what structural proteins?

A

Fibrous proteins

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25
Q

Actin and myosin are examples of what structural proteins?

A

Contractile Proteins (65% of muscle composition)

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26
Q

what are examples of fibrous proteins?

A

collagen
elastin
keratin

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27
Q

what are the examples of contractile proteins?

A

actin

myosin

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28
Q

Immunoglobulins and antibodies are examples of what biologically functional proteins?

A

Immunoproteins

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29
Q

what are the general examples of immunoproteins?

A

immunoglobulins, and antibodies

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30
Q

the Y-shaped proteins containing 4 proteins that binds to antigens and inactivate?

A

Immunoproteins

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31
Q

what are the five classes of immunoproteins?

A 
IgG
IgA
IgM
IE
IgD
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32
Q

the class of immunoproteins that is found in 75% of plasma?

A

IgG

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33
Q

The Class of immunoprotein that is in secretions such as (tears,saliva, and breast milk)?

A

IgA

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34
Q

The class of immunoprotein that was originally malaria and is a response to all antigens?

A

IgM

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35
Q

The class of immunoprotein that is for Allergies?

A

IgE

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36
Q

The class of immunoprotein for chronic infections?

A

IgD

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37
Q

The characteristics of IgG?

A

found in 75% of plasma

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38
Q

The characteristics of IgA?

A

found in secretions such as (tears, saliva, and breast milk)

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39
Q

The characteristics Of IgM?

A

originally malaria, and a response to all antigens

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40
Q

The characteristics of IgE?

A

the response to Allergies

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41
Q

The characteristics of IgD?

A

released during Chronic infections

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42
Q

the type of protein that has the biological function to combine with other susbstances and acts as a mode of transport through body?

A

Transport Proteins

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43
Q

what is the biological function of transport proteins?

A

to combine with other substances and acts as a mode of transport through the body

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44
Q

what are some examples of transport proteins?

A

Albumin
Hemoglobin
Transferrin
Vitamin D

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45
Q

Albumin, Hemoglobin, Transferrin, and Vitamin D are examples of what Biologically functional proteins?

A

Transport Proteins

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46
Q

Albumin is the Transport protein for what?

A

Calcium, Zinc, Vitamin B6

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47
Q

Hemoglobin is the transport protein for?

A

Oxygen

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48
Q

Transferrin is the transport protein for?

A

Iron

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49
Q

Vitamin D is the Transport Protein for?

A

Binding protein-Vitamin D

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50
Q

The type of protein that has the biological functions to be a biological catalyst, regulate metabolic pathways, limit rates, and is necessary for life?

A

ENZYMES!

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51
Q

what are the biological functions of enzymes?

A

Biological catalyst
Regulate Metabolic Pathways
limit rates of reactions
necessary for life

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52
Q

what are characteristics of Biological catalysts?

A
  • they speed up reaction by lowering activation energy needed for reaction to occur.
  • they are not used up during this process
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53
Q

Fluid Balance is an example of what?

A

a biological function of protein

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54
Q

Some ways that proteins regulate fluid balance?

A
  • water interacts with several groups on proteins
  • charged residues, peptide backbone, hydroxyl groups
  • water attracted to protein
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55
Q

some ways that a protein deficiency would affect the fluid balance biological function?

A

-Protein deficiency can cause fluid to leak into interstitial spaces causing Edema

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56
Q

what is Kwashiorkor?

A

a protein Malnutrition

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57
Q

what are some causes of a protein deficiency that would affect fluid balance?

A
  • Deficiency can be caused by kidney disease, large wounds, liver disease, and Malnutrition
  • Kwashiorkor- Protein Malnutrition
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58
Q

a biological function of proteins is to buffer? what is a buffer?

A

a compound that prevents a change in pH

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59
Q

Proteins act as buffers in?

A

plasma

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60
Q

Hemoglobin is a buffer in?

A

red blood cells

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61
Q

what is the buffer in red blood cells?

A

hemoglobin

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62
Q

What is the buffer in Plasma?

A

Proteins

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63
Q

what is a compound that prevents a change in pH?

A

Buffer

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64
Q

a protein Deficiency that can be caused by kidney disease, large wounds, liver disease, and Malnutrition would affect what biological function of proteins?

A

fluid balance

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65
Q

-water interacting with several groups on proteins
-charged residues, peptide backbone, hydroxyl groups
-water attracted to protein
are some of the ways that proteins perform what biological function?

A

Fluid Balance

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66
Q

buffers work when pH is?

A

pH is low (too many H+)

pH is High (too few H+)

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67
Q

When a base is added, what happens to the [H+]?

A

Decreases

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68
Q

when a base is added, which part of the protein donates a H+?

A

amino group

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69
Q

how many essential amino acids are there?

A

9 essential

must get from our diet (exogenous)

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70
Q

how many amino acids are non-essential?

A

11 non-essential

Body can make (endogenous)

71
Q

what does exogenous mean?

A

-must get from outside body.

from our diet

72
Q

what does endogenous mean?

A

-from inside our body

body can make

73
Q

Amino acids are the building block of?

A

proteins

74
Q

which isomer of an amino acid is corn spelled clockwise?

A

L-amino acids

75
Q

which isomer of an amino acid is corn spelled counter clockwise?

A

D- amino acids

76
Q

what percentage of amino acids found in the liver are used to make new proteins and N-containing compounds?

A

20%

77
Q

20% of amino acids found in the liver are used to make?

A

new proteins and N-containing compounds

78
Q

what are the new proteins made in the liver?

A

enzymes (remain in liver)
Plasma proteins
acute phase proteins (inflammatory response)

79
Q

what amino acids are used by the muscles?

A

Branched chain amino acids only

Valine, Leucine, and Isoleucine

80
Q

albumin, prealbumin, alpha-1 proteins, alpha-2 proteins, beta-globulins, Y-globulins are what type of proteins?

A

plasma proteins

81
Q

what are the plasma proteins?

A 
albumin
prealbumin
alpha-1 globulin
alpha-2 globulin
beta-globulin
Y-globulin
82
Q

what is the most abundant plasma protein, and maintains osmotic pressure. its a transport protein that is used to measure protein status?

A

albumin

83
Q

characteristics of the plasma protein albumin?

A
  • most abundant plasma protein
  • maintains osmotic pressure
  • transport nutrients
  • measure of protein status, but slow to change (2 weeks)
  • deficiency will cause Kwashiorkor
84
Q

what nutrients does albumin transport?

A 
vitamin B6
zinc
calcium
copper
smaller fatty acids
tryptophan
85
Q

vitamin B6, zinc, copper, calcium, smaller fatty acids, and tryptophan are transported by what plasma protein?

A

albumin

86
Q

a deficiency of which two plasma proteins would cause kwashiorkor?

A

albumin

prealbumin

87
Q

what is a transport protein, that is a measure of protein status with a half-life of 2 days?

A

prealbumin

88
Q

which plasma protein is a glycoprotein, high density lipoprotein?

A

alpha-1 globulins

89
Q

which plasma protein contains glycoprotein, haptoglobin, ceruloplasmin, prothrombin, and very low density lipoproteins?

A

alpha-2 globulins

90
Q

which plasma protein contains transferrin, and low density lipoproteins?

A

beta-globulins

91
Q

which plasma protein contains immunoglobulins?

A

Y-globulins

92
Q

what is the definition of non polar?

A

hates water (hydrophobic)

93
Q

the non-polar amino acids?

A 
Glycine
alanine
Valine
Leucine
Isoleucine
Methionine
Proline
Phenylalanine
tryptophan
94
Q

Glycine is what type of amino acid?

A

Non-Polar, and Aliphatic

95
Q

what is the definition of polar?

A

loves water (hydrophilic)

96
Q

serine is what type of amino acid?

A

Polar

97
Q

Alanine is what type of amino acid?

A

Non-Polar, and Aliphatic

98
Q

Theronine is what type of amino acid?

A

Polar

99
Q

Cysteine is what type of amino acid?

A

Polar

100
Q

Valine is what type of amino acid?

A

Non-Polar, and Aliphatic

101
Q

Leucine is what type of amino acid?

A

Non-Polar, and Aliphatic

102
Q

Isoleucine is what type of amino acid?

A

Non-Polar, and Aliphatic

103
Q

Tyrosine is what type of amino acid?

A

Polar, and Aromatic

104
Q

Asparagine is what type of amino acid?

A

Polar

105
Q

Glutamine is what type of amino acid?

A

Polar

106
Q

Methionine is what type of amino acid?

A

Non-Polar, and Aliphatic

107
Q

Proline is what type of amino acid?

A

Non-Polar, and Aliphatic

108
Q

Phenylalanine is what type of amino acid?

A

Non-Polar, and Aromatic

109
Q

Aspartate is what type of amino acid?

A

Polar, and Acidic

110
Q

Tryptophan is what type of amino acid?

A

Non-Polar, and Aromatic

111
Q

Glutamate is what type of amino acid?

A

Polar, and Acidic

112
Q

Lysine is what type of amino acid?

A

Polar, and Basic

113
Q

Arginine is what type of amino acid?

A

Polar, and Basic

114
Q

Histidine is what type of amino acid?

A

Polar, and Basic

115
Q

what is the definition of an Aliphatic amino acid?

A

contains a hydrocarbon chain in the R group

116
Q

what type of amino acid contains a hydrocarbon chin in the R group?

A

Aliphatic

117
Q

what is the definition of an Aromatic amino acid?

A

contains a 6 membered ring in the R group

118
Q

what type of amino acid has a 6 membered ring in the R group?

A

Aromatic

119
Q

what is the definition of an acidic Compound?

A

(negatively charged)

contains a carboxylic acid in the R group

120
Q

when an acid is added, which part of the protein accepts the H+?

A

carboxylic group

121
Q

what type of amino acid contains a carboxylic acid in the R group?

A

Acidic

122
Q

what type of amino acid contains an N in the R group?

A

Basic (positively charged)

123
Q

what is the definition of a Basic amino acid?

A

contains an N on the R group

124
Q

The characteristics of Glycine?

A 
Non-Polar (Aliphatic) uncharged
Only Amino Acid without a Chiral C
Found in high concentrations in collagen
allows bends in peptide
nonessential
125
Q 
Non-Polar (Aliphatic) uncharged
Only Amino Acid without a Chiral C
Found in high concentrations in collagen
allows bends in peptide
nonessential
which amino acid is this?
A

Glycine

126
Q

the characteristics of Alanine?

A

Non-Polar (Aliphatic) uncharged

Released from muscle during starvation, exercise, or after a high carbohydrate meal to be turned into glucose

127
Q

Non-Polar (Aliphatic) uncharged
Released from muscle during starvation, exercise, or after a high carbohydrate meal to be turned into glucose.
which amino acid is this?

A

Alanine

128
Q

what are the characteristics of Valine?

A

Non-Polar (Aliphatic) uncharged
Branched Chain Amino acid
Essential

129
Q

Non-Polar (Aliphatic) uncharged
Branched Chain Amino acid
Essential
which amino acid is this?

A

Valine

130
Q

what is the disease when Valine replaces glutamate in hemoglobin and causes red blood cells to fold incorrectly?

A

sickle cell anemia

genetic mutation that occured over time to protect against malaria

131
Q

what happens to cause sickle cell anemia?

A

Valine (nonpolar) replaces Glutamate (polar) in hemoglobin.

-causes red blood cells to fold incorrectly

132
Q

the characteristics of Leucine?

A

Nonpolar (Aliphatic), uncharged amino acid
Branched chain amino acid
essential
high concentration in globulin and albumin(hemoglobin)
partial degradation yields HMG Coa (precursor to cholesterol)

133
Q

-Nonpolar (Aliphatic), uncharged amino acid
-Branched chain amino acid
-essential
-high concentration in globulin and albumin(hemoglobin)
-partial degradation yields HMG Coa (precursor to cholesterol)
which amino acid is this?

A

Leucine

134
Q

what are the characteristics of Isoleucine?

A

Non-Polar (Aliphatic), uncharged AA
Branched Chain AA
Essential
Structural isomer of Leucine

135
Q 
Non-Polar (Aliphatic), uncharged AA
Branched Chain AA
Essential
Structural isomer of Leucine
which amino acid is this?
A

Isoleucine

136
Q

the disease when there is a genetic deficiency of enzymes required to metabolize branched chain amino acids?

A

Maple Syrup Urine Disease

Urine with color, odor, and viscosity of maple syrup

137
Q

the characteristics of maple syrup urine disease?

A
  • genetic deficiency of enzymes required to metabolize branched chain amino acids.(valine, leucine, Isoleucine)
  • Symptoms: urine with color, odor, and viscosity of maple syrup
  • if untreated can cause brain damage and health
  • treatment: avoid high protein food for life
138
Q

what are the characteristics of Methionine?

A 
Nonpolar (Aliphatic) uncharged
essential
S-containing
Precursor for:
-S-adenosyl methionine (SAMe)
-Cysteine
139
Q 
Nonpolar (Aliphatic) uncharged
essential
S-containing
Precursor for:
-S-adenosyl methionine (SAMe)
-Cysteine
which amino acid is this?
A

Methionine

140
Q

the function of SAMe in the body?

A

methylates compounds

141
Q

SAMe is required by the body to make?

A 
Carnitine
creatine
epinephrine
melatonin
glutathione
taurine
myelin basic protein
142
Q

SAMe may be used to treat?

A

osteoarthritis, depression

143
Q

Populations who should not use SAMe?

A

those with bipolar disorder
patients on antidepressants
cancer patients

144
Q

what are the characteristics of Proline?

A
  • nonpolar, uncharged amino acid
  • Not aromatic
  • nonessential
  • disrupts alpha-helix and beta pleated sheet structure.
  • found in high concentrations in collagen
145
Q

-nonpolar, uncharged amino acid
-Not aromatic
-nonessential
-disrupts alpha-helix and beta pleated sheet structure.
-found in high concentrations in collagen
which amino acid is this?

A

proline

146
Q

what are the characteristics of phenylalanine?

A

nonpolar (aromatic), uncharged AA
essential
precursor for tyrosine

147
Q

nonpolar (aromatic), uncharged AA
essential
precursor for tyrosine
which amino acid is this?

A

phenylalanine

148
Q

what is the genetic disorder that lacks enzyme necessary to metabolize phenylalanine?

A

phenylketonuria

149
Q

what are the characteristics of Phenylketonuria?

A
  • genetic disorder that lacks enzyme necessary to metabolize phenylalanine
  • causes brain damage
  • 1/10,000 babies born with
  • Phenylalanine found in Nutrasweet and anything with protein
  • Treatment: avoid Phenylalanine in diet (low protein)
150
Q

what is the genetic disorder where you are missing 1 phenylalanine in protein that regulates transport of chloride ions across cell membranes?

A

Cystic Fibrosis

most common genetic disorder

151
Q

the characteristics of Cystic Fibrosis?

A
  • genetic disorder affecting 1/2,000 humans
  • missing 1 phenylalanine in protein that regulates transport of chloride ions across a cell membrane
  • does not fold correctly, protein is degraded
  • causes mucus to build up (lung and digestion issues)
152
Q

what are the characteristics of Tryptophan?

A 
nonpolar (aromatic) uncharged AA
essential
precursor for:
-serotonin
-melatonin
-Niacin
153
Q 
nonpolar (aromatic) uncharged AA
essential
precursor for:
-serotonin
-melatonin
-Niacin
which amino acid is this?
A

Tryptophan

154
Q

the neurotransmitter needed for mood, behavior, Body T, and appetite?

A

serotonin

155
Q

the hormone needed for biological clock and acts as an antioxidant?

A

Melatonin

156
Q

what are the characteristics of Serine?

A

polar, uncharged AA

  • nonessential
  • important in active site of enzymes
  • able to H-Bond
  • Hydroxyl group is Phosphorylated for protein regulation
157
Q 
polar, uncharged AA
-nonessential
-important in active site of enzymes
-able to H-Bond
-Hydroxyl group is Phosphorylated for protein regulation
which amino acid is this?
A

Serine

158
Q

what are the characteristics of Threonine?

A

Polar, uncharged AA

  • essential
  • also a site of phosphorylation in protein regulation
159
Q

Polar, uncharged AA
-essential
-also a site of phosphorylation in protein regulation
which amino acid is this?

A

threonine

160
Q

what are the characteristics of Cysteine?

A

Polar, uncharged AA

  • nonessential
  • thiol (SH) group is a proton donor in GLUTATHIONE
  • antioxidant properties
  • important in proteins that participate in REDOX
  • important for cross-linking proteins through disulfide bonds
161
Q

Polar, uncharged AA
-nonessential
-thiol (SH) group is a proton donor in GLUTATHIONE
-antioxidant properties
-important in proteins that participate in REDOX
-important for cross-linking proteins through disulfide bonds
which amino acid is this?

A

Cysteine

162
Q

Albumin and insulin are 2 of many proteins stabilized by?

A

(Cystine) disulfide bridges

163
Q

what are the characteristics of Tyrosine?

A 
Polar, uncharged AA
-nonessential
-precursor for:
thyroid hormones (thyroxine)
Melanin (pigment)
-Catecholamines
dopamine
norepinephrine
epinephrine
164
Q

the catecholamine that relates to mood, behavior, and cognition?

A

Dopamine

165
Q

Dopamine is a catecholamine that controls what?

A

mood, behavior, cognition

166
Q

what is the catecholamine that is a derivative of tyrosine and is a stress hormone?

A

Norepinephrine

167
Q

Norepinephrine is what type of hormone?

A

stress hormone

168
Q

what is the catecholamine responsible for fight or flight?

A

Epinephrine

169
Q

Epinephrine is responsible for what?

A

fight or flight

170
Q

what are the characteristics of Asparagine?

A

Polar, uncharged Amino Acid

  • found at the beginning an d end of alpha-helix because of H-bonding in R-Group
  • forms acrylamide with sugar at high temperature.
171
Q

Polar, uncharged Amino Acid
-found at the beginning an d end of alpha-helix because of H-bonding in R-Group
-forms acrylamide with sugar at high temperature.
what is this amino acid?

A

Asparagine

172
Q

HCL denatures what protein structures?

A

2, 3 , and 4 structures of proteins

173
Q

is the globular class of protein shape polar or non-polar?

A

polar

174
Q

the shape of this protein is decided by secondary, tertiary, and quaternary?

A

globular

Biochemistry 1 (4 decks)

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