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Biochem 1 > Exam 2 > Flashcards

Exam 2 Flashcards

1
Q

Biological Functions of Proteins

A
  • Signaling Compounds and Receptors, * Structural Proteins, * Immunoproteins,* Transport Proteins, * Enzymes, * Fluid Balance, * Buffers, * Other (e.g. storage proteins)
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2
Q

Peptide Hormones

A

> 100 amino acids (e.g. Glucagon, Parathyroid Hormone, Calcitonin, Insulin, Oxytocin).

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3
Q

AA (Amino Acid) Derivative

A

1 amino acid (e.g. Tyrosine, Histidine, Tryptophan).

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4
Q

Tyrosine (Derivatives)

A

Thyroid hormones (thyroxine), catecholamines (dopamine, epinephrine, and norepinephrine)

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5
Q

Histidine (Derivatives)

A

Histamine (immune response associated with allergies)

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6
Q

Tryptophan (Derivatives)

A

Serotonin (neurotransmitter regulating mood, sleep, appetite), melatonin (regulates sleep-wake cycle)

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7
Q

Cytokines

A

Small proteins that act as regulators of growth and differentiation (e.g. Interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-α), IL-6, C-reactive protein (CRP), and IL-10).

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8
Q

Interleukin-10

A

Anti-inflammatory cytokine produced during exercise.

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9
Q

C-reactive Protein (CRP)

A

The cytokine that is the best indicator of inflammation.
Biomaker
* good < 1 mg/dL, * mid 1-3 mg/dL, * high > 3 mg/dL, * rheumatoid arthritis > 60 mg/dL

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10
Q

Baseline Inflammation

A

25% of {this} is due to phagocytes trapped in our adipose tissue.

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10
Q

Fibrous Proteins

A

Collagen, Elastin, Keratin

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11
Q

Contractile Proteins

A

(65% of muscles) Actin, Myosin

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12
Q

Immunoproteins

A

(Immunoglobulins, Antibodies) Y-shaped proteins containing 4 peptides that bind to antigens and inactivate (e.g. five classes: IgG, IgA, IgM, IgE, and IgD).

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13
Q

IgE

A

Immunoprotein class responsible for allergies.

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14
Q

Transport Proteins

A

Proteins that combine with other substances and acts as a mode of transport through the body (e.g. albumin, hemoglobin, transferrin, and vitamin d-binding protein).

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15
Q

Albumin (Transport Protein)

A

Transport protein that transports calcium, zinc, and vitamin B₆. Maintains osmotic pressure. Three-quarters of all protein in the plasma. Can be used to measure protein status, but is slow to change (~2 weeks).

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16
Q

Hemoglobin (Transport Protein)

A

Transport protein that transports oxygen.

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17
Q

Transferrin (Transport Protein)

A

Transport protein that transports iron.

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18
Q

Vitamin D-binding Protein (Transport Protein)

A

Transport protein that transports Vitamin D.

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19
Q

Enzymes

A

Biological catalysts that speed up reactions by lowering energy needed for reaction to occur and are not used up in the process.

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20
Q

Fluid Balance

A

Water interacts with several groups on proteins: charged residues, peptide backbone, and hydroxyl groups. Water is attracted to protein. A protein deficiency can cause edema.

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21
Q

Kwashiorkor

A

Protein malnutrition.

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22
Q

Buffer

A

A compound that prevents a change in pH (e.g. hemoglobin in RBCs).

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23
Q

Amino Acids

A

Building blocks of proteins. 9 essential (i.e. need in our diet (exogenous)), 11 nonessential (i.e. our body can make (endogenous)).

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24
Q

AA (Amino Acid) Structure

A

Positively charged amino group (NH₃⁺), side chain, negatively charged carboxyl group (COO⁻) all attached to an α-carbon.

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25
Q

AA (Amino Acids) Metabolized in Liver

A

20% of amino acids in the liver are used to make new proteins and N-containing compounds. New proteins made: enzymes (remain in liver), plasma proteins, acute phase proteins (inflammatory response).

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26
Q

Branched Chain (Amino Acids Metabolized)

A

{These} types of amino acids are metabolized in muscles.

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27
Q

Prealbumin

A

A transport protein with a half-life of 2 days. Best biomarker for protein.

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28
Q

Glycine

A
  • Nonessential, * Nonpolar, * Glucogenic, * Found in high concentrations in collagen, * Simplest amino acid
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29
Q

Proline

A
  • Nonessential, * Nonpolar, * Glucogenic, * Found in high concentrations in collagen
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30
Q

Alanine

A

*Nonessential, * Nonpolar, * Glucogenic

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31
Q

Valine

A
  • Essential, * Nonpolar, * Glucogenic, * Branched Chain
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32
Q

Methionine

A
  • Essential, * Nonpolar, * Glucogenic, * Precursor for SAMe
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33
Q

Phenylalanine

A
  • Essential, * Nonpolar, * Both Glucogenic and Ketogenic, * Aromatic
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34
Q

Isoleucine

A
  • Essential, * Nonpolar, * Both Glucogenic and Ketogenic,* Branched Chain
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35
Q

Tryptophan

A
  • Essential, * Nonpolar, * Both Glucogenic and Ketogenic, * Aromatic, * Precursor for Serotonin, Melatonin, Niacin
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36
Q

Leucine

A
  • Essential, * Nonpolar, * Ketogenic, * Branched Chain, * Precursor for Cholesterol
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37
Q

Cysteine

A
  • Nonessential, * Polar, * Glucogenic, * Important for cross-linking proteins through disulfide bonds (i.e. Disulfide Bridge)
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38
Q

Asparagine

A
  • Nonessential, * Polar, * Glucogenic
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39
Q

Glutamine

A
  • Nonessential,* Polar,* Glucogenic,* Main N Carrier
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40
Q

Serine

A
  • Nonessential,* Polar,* Glucogenic,* Able to H-bond
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41
Q

Aspartic Acid

A
  • Nonessential, * Polar,* Glucogenic, * Acidic
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42
Q

Glutamic Acid

A
  • Nonessential, * Polar,* Glucogenic, * Acidic, * Precursor for GABA (gamma-amino butyric acid)
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43
Q

Arginine

A
  • Nonessential, * Polar, * Glucogenic,* Basic,* Precursor for Nitric Oxide (NO) (a vasodilator)
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44
Q

Histidine

A
  • Essential,* Polar,* Glucogenic,* Basic,* Precursor for Histamine
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45
Q

Threonine

A
  • Essential, * Polar, * Both Glucogenic and Ketogenic
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46
Q

Tyrosine

A
  • Nonessential, * Polar, * Both Glucogenic and Ketogenic, * Aromatic, * Precursor for Thyroid Hormones, Melanin, Catecholamines
47
Q

Lysine

A
  • Essential, * Polar, * Ketogenic, * Basic, * Important for collagen formation
48
Q

Essential AA (Amino Acids)

A

PVT MT HILL: Phenylalanine, Valine, Tryptophan, Methionine, Threonine, Histidine, Isoleucine, Lysine, Leucine

49
Q

Glucogenic

A

Amino acid is used to make glucose if necessary (product: pyruvate).

50
Q

Ketogenic

A

Amino acid is turned into Kreb’s cycle intermediate, ketone bodies, or fatty acids if in excess (product: acetyl CoA).

51
Q

Ketogenic Only

A

Leucine and Lysine

52
Q

Glucogenic and Ketogenic

A

Phenylalanine, Isoleucine, Tryptophan, Threonine, and Tyrosine

53
Q

Branched Chain AA (Amino Acids)

A

Valine, Isoleucine, and Leucine

54
Q

Aromatic AA (Amino Acids)

A

Phenylalanine, Tryptophan, and Tyrosine

55
Q

Acidic AA (Amino Acids)

A

Aspartic Acid and Glutamic Acid

56
Q

Basic AA (Amino Acids)

A

Arginine, Histidine, and Lysine

57
Q

Sickle Cell Anemia

A
  • Genetic disorder, * Valine (nonpolar) replaces Glutamate (polar) in hemoglobin, * Protein folds incorrectly
58
Q

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, * Untreated: brain damage and death, * Treatment: avoid high protein food
59
Q

Phenylketonuria (PKU)

A
  • Genetic disorder that lacks enzyme necessary to metabolize phenylalanine, * Causes brain damage, * Phenylalanine found in Nutrasweet and anything with protein, * Treatment: avoid phenylalanine
60
Q

Cystic Fibrosis

A
  • Genetic disorder affecting 1 in 2000, * Missing 1 phenylalanine in protein that regulates transport of chloride ions across cell membranes, * Protein does not fold correctly, protein is degraded, * Causes mucus to build up (lung and digestion issues)
61
Q

Coenzymes/Cofactors (in AA Metabolism)

A

Vitamin C, Vitamin B₆, Folic Acid, Iron, Niacin function as {these} in AA metabolism.

62
Q

pK

A

The acid dissociation constant.

63
Q

pK₁

A

The removal of H from the carboxyl group acid dissociation constant.

64
Q

pK₂

A

The removal of H from the amino group acid dissociation constant.

65
Q

pK-R

A

The removal of H from the R group acid dissociation constant.

66
Q

Protonated

A

Has hydrogen (H) attached (e.g. pH < pK).

67
Q

Deprotonated

A

Hydrogen (H) lost (e.g. pH > pK).

68
Q

Isoelectric Point (pI)

A
  • The point where an AA or protein is neutral (zwitterion), * when pH < pI, then protein has a net positive charge, * when pH > pI, then protein has a net negative charge
69
Q

pI (Calculation)

A
  • average of pK₁ and pK₂ (AA without any loss from R-group), * average of pK-R and the closest pK (AA with loss from potential from R-group(s))
70
Q

Physiologic pH

A

7.4

71
Q

Amphoteric

A

Compound that can act as an acid and a base.

72
Q

Peptides

A
  • Chains of AA, * Formed via condensation/dehydration reactions, * Bonds trans in nature
73
Q

Dipeptide

A

2 amino acid peptide.

74
Q

Polypeptide

A

Peptide of 10-100 amino acids.

75
Q

Protein

A

Peptide of > 100 amino acids.

76
Q

Primary (1°) (Protein Structure)

A
  • Sequence of amino acids, * Includes covalent bonding (peptide bonds), * Sequence determines other structural levels and acts as signals, * Does not change during denaturation
77
Q

Secondary (2°) (Protein Structure)

A
  • Spatial arrangement of atoms around a polypeptide backbone, * Stabilized by noncovalent interactions (IMF, mostly H-bonding), * α-helices, β-pleated sheets, and β-bends
78
Q

α-Helix

A

Repeat units of protein structure stabilized by H-bonding every 4 amino acids. H-bond between H on amide and O on carboxyl group of another amino acid.

79
Q

β-Sheet

A

Polypeptide H-bonded to another polypeptide aligned in parallel or antiparallel fashion.

80
Q

β-Bends

A

Reverse direction of polypeptide chain to fold compactly in globular structures (4 AA per turn). H-bond between carboxyl group on AA₁ and amide group on AA₄.

81
Q

Tertiary (3°) (Protein Structure)

A
  • 3-D arrangement, * Folding of peptide chains, * Influenced by R-groups, - Covalent Bonds (Disulfide Bonds between Cysteines), - Non-covalent Bonds (IMF)
82
Q

Quaternary (4°) (Protein Structure)

A
  • Grouping of 2+ peptide chains, * Non-covalent bonding (IMF), * Polar outside, nonpolar inside (so it can travel through aqueous liquids (blood))
83
Q

Globular (Protein Shape)

A
  • Highly folded, water-soluble proteins,* Dense, hydrophobic core, * Hydrophilic outside, * Easily denatured, * Hemoglobin, Myoglobin, Peptide Hormones (e.g. insulin, glucagon, oxytocin), Enzymes
84
Q

Fibrous (Protein Shape)

A
  • Long strands of proteins, highly cross-linked, * Insoluble, * Structural role of the body, * Hard to denature, * Keratin (hair, nails), Elastin (connective tissue), Collagen (connective tissue)
85
Q

Collagen

A
  • Triple helix, * Extracellular matrix of bone and connective tissue, * One-third of total protein in the body, * Glycine - Proline - Y and Glycine - X - Hydroxyproline, - X and Y can be any amino acid; often hydroxylysine, - Vitamin C required to hydroxylate proline and lysine
86
Q

Hydroxy-

A

Nomenclature prefix denoting the addition of a hydroxyl (-OH) group. The addition of which adds a H donor and acceptor key to H-bonding.

87
Q

Scurvy

A
  • Vitamin C deficiency, * Symptoms: corkscrew hairs, bleeding gums
88
Q

Complete Proteins

A
  • Foods that contain all essential AA, * Animal proteins (e.g. human milk, eggs, meat, poultry, seafood, dairy; EXPECT gelatin), * Plant proteins: soy, amaranth, quinoa
89
Q

Incomplete Proteins

A
  • Foods that do not contain all essential AA, * Corn - deficient in lysine and tryptophan, * Wheat - deficient in lysine, * Rice - deficient in lysine, * Legumes (beans, peanuts, peas) - deficient in methionine
90
Q

Complimentary Proteins

A

Combining 2 incomplete proteins that together provide all 9 essential AA.

91
Q

4 kcal / gram

A

Caloric value of protein per gram.

92
Q

(Protein Digestion in) Mouth

A

No protein digestion occurs here (before stomach).

93
Q

(Protein Digestion in) Stomach

A
  • HCl is released from parietal cells in response to gastrin (which is released due to organ distention, smell, thought, and/or sight of food), - Denatures 2°, 3°, and 4° structured proteins, - Converts pepsinogen (inactive enzyme released by chief cells) to pepsin (active)
94
Q

Pepsin

A

An endopeptidase found in the stomach.

95
Q

Endopeptidase

A

An enzyme that breaks internal peptide bonds in a peptide chain which results in polypeptides, oligopeptides (maximum 3 AA long), and free AA.

96
Q

Exopeptidase

A

An anzyme that breaks the terminal peptide bond in a peptide chain resulting in free AA only.

97
Q

(Protein Digestion in) Small Intestine

A
  • Chyme released {here} stimulates release of secretin and CCK (cholecystokinin), * Secretin and CCK stimulate release of bicarbonate, water, electrolytes, and zymogens from pancreas
98
Q

Trypsinogen

A

Pancreatic zymogen of Trypsin. Activated by Enterokinase or Trypsin.

99
Q

Chymotrypsinogen

A

Pancreatic zymogen of Chymotrypsin. Activated by Trypsin.

100
Q

Procarboxypeptidase

A

Pancreatic zymogen of Carboxypeptidase. Activated by Trypsin.

101
Q

Proelastase

A

Pancreatic zymogen of Elastase. Activated by Trypsin.

102
Q

Pancreatic Endopeptidases

A

Trypsin, Chymotrypsin, Elastase, and Collagenase

103
Q

Elastase

A

Pancreatic endopeptidase that digests protein in elastin.

104
Q

Collagenase

A

Pancreatic endopeptidase that digests protein in collagen.

105
Q

Pancreatic Exopeptidase

A

Carboxypeptidase

106
Q

Carboxypeptidase

A

Pancreatic exopeptidase that digests protein from the carboxy terminal and is zinc dependent.

107
Q

Brush Border Endopeptidase

A

Enterokinase

108
Q

Enterokinase

A

Brush border endopeptidase that activates trypsin.

109
Q

Brush Border Exopeptidases

A

Aminopeptidase, Dipeptidase

110
Q

Aminopeptidase

A

Brush border exopeptidase that digests protein from the amino terminal.

111
Q

Dipeptidase

A

Brush border exopeptidase that digests peptide bond between 2 amino acids in a dipeptide and is magnesium dependent.

112
Q

(Protein Digestion in) Large Intestine (Colon)

A

No digestion occurs here (after small intestine).

113
Q

Free AA (Absorption)

A
  • Absorbed via active transport utilizing AA Transporter, Na⁺, K⁺, and ATP, * Sodium binds carrier protein → AA binds carrier protein → carrier protein release sodium and AA inside enterocyte → sodium is pumped out of enterocyte and potassium is pumped in using ATP
114
Q

Peptide (Absorption)

A
  • Absorbed via active transport utilizing PEPT1 transport protein, H⁺, Na⁺, K⁺, and ATP, * Hydrogen binds to PEPT1 → di/tri peptide binds to PEPT1 → PEPT1 release hydrogen and di/tri peptide inside enterocyte → hydrogen is pumped back into the SI lumen in exchange for sodium → sodium is pumped out of enterocyte and potassium is pumped in using ATP → peptidase (enzyme in the cytoplasm) digests di/tri peptides to free AA so they can cross the basolateral membrane
115
Q

(AA in) Enterocytes

A
  • AA are used for energy or protein synthesis, * AA {here} are necessary to make: - Proteins for new {these}, - Nucleotides, - Apoproteins for lipoproteins, - New digestive enzymes, - Hormones, - N-containing compounds
116
Q

AA Transport Out of Enterocyte

A

Free AA not needed by the enterocyte are transported through the basolateral membrane into the interstitial fluid by passive diffusion and facilitated diffusion (AA Transporter).

Biochem 1 (2 decks)

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