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Biochemistry 1 > exam 2 review > Flashcards

exam 2 review Flashcards

1
Q

what are the 7 functions of proteins?

A 
signaling
structure
immunity
buffer
enzymes
transport
fluid balance
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2
Q

what are examples of inflammatory cytokines?

A

C-Reactive Protein
Interleukin-6
interleukin-1
tumor necrosis factor- alpha

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3
Q

what are examples of an anti-inflammatory cytokine?

A

interleukin-10

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4
Q

what is a peptide hormone?

A

made up of multiple amino acids

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5
Q

what is an AA derivative?

A

made up from a single amino acid

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6
Q

what is the difference between a peptide hormone and an amino acid derivative?

A

peptide hormones are made up from multiple amino acids and derivatives are made up from a single amino acid

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7
Q

which immunoglobulin is used to test for allergies?

A

IgE

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8
Q

Are Amino Acids naturally found in the D or L isomer?

A

L isomer

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9
Q

where are most amino acids metabolized in the body?

A

Liver

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10
Q

what are some examples of proteins made in the liver?

A

Enzymes (remain in liver)
Plasma proteins
Acute Phase Proteins (inflammatory response)

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11
Q

which plasma proteins are used to measure a protein deficiency?

A

albumin

prealbumin

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12
Q

list the 9 essential amino acids?

A 
phenylalanine
valine
tryptophan
methionine
threonine
histidine
isoleucine
lysine
leucine
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13
Q

what are the ketogenic amino acids?

A

Leucine

Lysine

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14
Q

what are the Glucogenic Amino acids?

A 
Glycine
Alanine
Proline
Valine
Methionine
Theronine
Histidine
Cysteine
Asparagine
Glutamine
Serine
Aspartic Acid
Glutamic Acid
Arginine
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15
Q

what are the amino acids are both ketogenic and Glucogenic?

A

Phenylalanine
isoleucine
tryptophan
tyrosine

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16
Q

what are the polar amino acids?

A 
Cysteine
asparagine
glutamine
serine
apartic acid
glutamic acid
arginine
theronine
histidine
lysine
tyrosine
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17
Q

what are the aromatic amino acids?

A

phenynlalanine
tryotophan
tyrosine

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18
Q

what are the non polar amino acids?

A 
glycine
alanine
proline
valine
methionine
phenylalanine
isoleucine
tryptophan
leucine
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19
Q

what are the three branched chain amino acids?

A

Leucine
Isoleucine
Valine

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20
Q

where are the branched chain metabolized?

A

muscles

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21
Q

which amino acid is a precursor to cholesterol?

A

Leucine

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22
Q

which amino acid is a precursor to serotonin?

A

tryptophan

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23
Q

which amino acid is a precursor to dopamine?

A

Tyrosine

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24
Q

which amino acid is a precursor to Thyroxine?

A

Tyrosine

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25
Q

which amino acid is a precursor to Niacin?

A

Tryptophan

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26
Q

which amino acid is a precursor to GABA?

A

Glutamic acid

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27
Q

which amino acid is a precursor to nitric oxide?

A

Arginine

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28
Q

which CoFactors and coenzymes are necessary for amino acid metabolism?

A 
Vitamin C
Vitamin B6
folic acid
iron
niacin
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29
Q

Which Amino acids disrupt secondary structures?

A 
Proline
Glutamate
aspartate
histidine
lysine
arginine
tryptophan
valine
isoleucine
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30
Q

what are the two sulfur containing amino acids?

A

methionine

cysteine

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31
Q

what is formed when two cysteine bind together?

A

sulfide bridge

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32
Q

why are serine and theronine important?

A

needed for phosphorylation to regulate protein

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33
Q

which amino acid is important in buffering?

A

histidine

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34
Q

why would cell recycling occur?

A

misfolding
damage by free radical or oxidation
not needed

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35
Q

explain the primary level of protein structure?

A
  • sequence of amino acids
  • includes covalent bonding
  • sequence determines 2 and 3 sructures and acts as signals
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36
Q

explain the secondary level of protein structure?

A

stabilized by nonconvalent interactions (IMF)
alpha-helix
Beta pleated sheets
Beta- bends
most proteins have a mixture of 2 structures

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37
Q

explain the tertiary level of protein structure?

A 
3-D arrangement
influenced by R-groups
Covalent bonds
-disulfide bonds
Noncovalent
-H.Bonds, ionic interactions, LDF
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38
Q

explain the quartenary level of protein structure?

A 
Grouping of 2+ peptide chains
Noncovalent interactions (IMF)
H-bonds
ionic interactions
LDF
Hemogobin-4 peptide chains
alcohol dehydrogenase
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39
Q

which reaction mechanism is used in peptide bond formation?

A

condensation/dehydration

40
Q

which pK is most important for the buffering capacity of proteins?

A

pKr

41
Q

which IMF is important for stabilizing secondary structures?

A

Noncovalent interactions

H-Bonds

42
Q

Which amino acids are often found in beta-bonds?

A

proline

glycine

43
Q

which covalent interaction is involved in the tertiary structure?

A

Disulfide bonds

44
Q

what do chaperone proteins help with?

A

they aid in protein folding.

  • keep protein unfolded until synthesis is complete
  • Act as catalysts for folding
  • Prevent getting tangled during folding
45
Q

how do heat, pH and mechanical shearing affect protein structure?

A

they unfold them

46
Q

compare globular and fibrous proteins?

A 
Globular
-highly folded, water soluble proteins
-dense, hydrophobic core
-hydrophilic outside
-easily denatured 
Fibrous
-long strands of proteins, highly cross-linked
-Insoluble
-structural role in body
-EX. Keratin, Elastin, Collagen
47
Q

what holds oxygen in the heme structure?

A

Iron

48
Q

where is myoglobin located?

A

muscles and heart

49
Q

how many peptide chains does myoglobin have?

A

1

50
Q

how many oxygens can myoglobin carry?

A

1

51
Q

where is hemoglobin located?

A

red blood cells

52
Q

how many peptide chains does hemoglobin have?

A

4

53
Q

how many oxygens can hemoglobin carry?

A

4

54
Q

compare R and T hemoglobin?

A 
relaxed
-oxyhemoglobin
-pKr in histidine is slightly lower
-Less ionic and H-bonds
-increase in oxygen or pH
Taut
-pKr in histidine is higher
-More ionic and H-Bonds
-Decrease in pH
55
Q

what is cooperative binding?

A

in Hemoglobin= binding o2 at one heme increases affinity for binding o2 at other heme sites-
-allows Hb to respond to small changes in oxygen conc.< peripheral tissues= oxyHb releases oxygen (unloads)

56
Q

what effect will pH, CO2, CO, and 2,3-biphosphoglycerate have on hemoglobin?

A

will effect the heme to heme bonds

57
Q

is the pH higher in the lungs or peripheral tissues?

what does this mean for oxygen loading/unloading?

A

Lungs

58
Q

under what conditions do we make 2,3 biphosphoglycerate?

A

concentration in RBC increases due to chronic hypoxia

59
Q

how many polypeptides does collagen have?

A

3 polypeptides

60
Q

which amino acids are found in the highest concentration in collagen?

A

proline
glycine
lysine

61
Q

what is the difference between fibril-forming and network forming collagen?
which is found in higher concentrations in bone?

A

network forming is a 3D-mesh most common IV

Fibril forming= rope like triple helix, common 1

62
Q

what is the most common type of collagen in the human body?

A

type 1

63
Q

what post-translational modification is important to the structure of collagen?

A

proline and vitamin C
Proline hydroxlase
post mod= functional group added after protein is synthesized

64
Q

which coenzyme and cofactor are important in the posttransational modification?

A

vitamin C is the CoEnzyme

Iron is the CoFactor

65
Q

why is glycosylation important?

A

allows hydroxylysine to bind to glucose and galactose. some proteins do not fold correctly unless glycosylated first.

66
Q

what does lysyl oxidase do? what is the cofactor for this reaction?

A

the CoFactor is Copper

  • Deanimates lysine forming reactive aldehyde
  • Aldehyde condenses with lysine or hydroxylysine on neighboring collagen
67
Q

what are MMPs?

A

Matrix metalloproteinases

  • main class of proteases
  • Metallo= requires (Ca & Zn)
68
Q

what pathways are MMPs involved in?

A 
degenerative disc disease
inflammation
cancer
wound healing
osteoarthritis
atherosclerosis
rheumatoid arthritis 
ulcers
endometriosis
69
Q

where is elastin found?

A

found in the lungs
large arteries
and elastic ligaments

70
Q

why might smoking be bad for the lungs?

A

smoking inhibits alpha1-antitrypsin (alpha1-AT), which is important for maintaining lung elasticity

71
Q

what is a holoenzyme?

A

Complete (active) enzyme

72
Q

what is a zymogen?

A

enzyme precursor (inactive enzyme)

73
Q

identify cofactors?

A

inorganic component needed to work
Fe, Mg, Zn, Se
Minerals

74
Q

identify CoEnzymes?

A

organic component needed to work
Vit. B6, Vit B12, thiamin, Folate, riboflavin, biotin, niacin
VITAMINS

75
Q

identify the 6 classes of enzymes for a given reaction?

A 
Oxidoreductase
transferase
isomerase
hydrolase
lyase
ligase
76
Q

describe how enzymes speed up reactions?

A

they lower the activation energy

77
Q

what kind of active site is the most common?

A

Induced-Fit Model

78
Q

how do temperature and pH affect enzyme activity?

A
  • increase of temperature, will increase rate of enzyme catalyzed reaction
  • eventually Temp. will denature
  • each enzyme has an optimal pH, depends on pK
  • Peak activity at Optimal pH
79
Q

what are the other factors that affect enzyme activity?

A

Enzyme and substrate conc.
-excess substrate-velocity of reaction depends on [E]
CoFactor/CoEnzymes
-vitamin or mineral deficiencies will decrease enzyme activity
Effectors
-Activators-increase activity
-Inhibitors- decrease activity

80
Q

describe how inhibitors affect Vmax and Km

A

S and I will compete for active site.
[S] will affect Km and Vmax
Inhibitors will affect Vmax only

81
Q

determine which portion of the kinetics curve is dependent on substrate and/or enzyme concentration?

A

look at graph

82
Q

what is the difference between a reversible and irreversible inhibitor?

A 
Irreversible
-Covalent bonding
-Must make more enzyme to make product
Reversible
-Noncovalent interactions
Can dissociate
competitive
noncompetitive
83
Q

what are allosteric enzymes?

A

-Regulatory enzymes in a cascade

Rate-limiting

84
Q

what is a negative and positive effector?

A

Negative Effector
-Feedback inhibition
-build up of product turns off allosteric enzyme
Positive Effector
-build up of substrate speeds up the reaction
-increases enzyme activity

85
Q

what is added/removed during covalent modification?

A

phosphate group to serine, theronine or tyrosine

86
Q

what is enzyme induction?

A
  • cells can regulate the amount of E induction or repression
  • synthesized at rates dictated by cellular circumstances
  • induction occurs from hormones and diet
  • EX. insulin (stimulates an increase in enzymes needed to metabolize glucose)
87
Q

describe protein digestion from mouth to excretion?location?

A

s

88
Q

list the enzymes involved in protein digestion?Location?

A

s

89
Q

list the secretions involved with protein digestion? location?

A

s

90
Q

list the hormones involved in protein digestion?Location?

A

s

91
Q

what is the difference between an exopeptidase and an endopeptidase?

A

s

92
Q

how are the zymogens activated in the stomach and SI?

A

s

93
Q

describe amoino acid and peptide absorption into the enterocyte?

A

s

94
Q

How are the Amino acids transported across the basolateral membrane?

A

s

95
Q

what is Apoenzyme?

A

protein part of enzyme only

Biochemistry 1 (4 decks)

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