exam 2 review Flashcards
1
Q
what are the 7 functions of proteins?
A
signaling structure immunity buffer enzymes transport fluid balance
2
Q
what are examples of inflammatory cytokines?
A
C-Reactive Protein
Interleukin-6
interleukin-1
tumor necrosis factor- alpha
3
Q
what are examples of an anti-inflammatory cytokine?
A
interleukin-10
4
Q
what is a peptide hormone?
A
made up of multiple amino acids
5
Q
what is an AA derivative?
A
made up from a single amino acid
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
7
Q
which immunoglobulin is used to test for allergies?
A
IgE
8
Q
Are Amino Acids naturally found in the D or L isomer?
A
L isomer
9
Q
where are most amino acids metabolized in the body?
A
Liver
10
Q
what are some examples of proteins made in the liver?
A
Enzymes (remain in liver)
Plasma proteins
Acute Phase Proteins (inflammatory response)
11
Q
which plasma proteins are used to measure a protein deficiency?
A
albumin
prealbumin
12
Q
list the 9 essential amino acids?
A
phenylalanine valine tryptophan methionine threonine histidine isoleucine lysine leucine
13
Q
what are the ketogenic amino acids?
A
Leucine
Lysine
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
15
Q
what are the amino acids are both ketogenic and Glucogenic?
A
Phenylalanine
isoleucine
tryptophan
tyrosine
16
Q
what are the polar amino acids?
A
Cysteine asparagine glutamine serine apartic acid glutamic acid arginine theronine histidine lysine tyrosine
17
Q
what are the aromatic amino acids?
A
phenynlalanine
tryotophan
tyrosine
18
Q
what are the non polar amino acids?
A
glycine alanine proline valine methionine phenylalanine isoleucine tryptophan leucine
19
Q
what are the three branched chain amino acids?
A
Leucine
Isoleucine
Valine
20
Q
where are the branched chain metabolized?
A
muscles
21
Q
which amino acid is a precursor to cholesterol?
A
Leucine
22
Q
which amino acid is a precursor to serotonin?
A
tryptophan
23
Q
which amino acid is a precursor to dopamine?
A
Tyrosine
24
Q
which amino acid is a precursor to Thyroxine?
A
Tyrosine
25
which amino acid is a precursor to Niacin?
Tryptophan
26
which amino acid is a precursor to GABA?
Glutamic acid
27
which amino acid is a precursor to nitric oxide?
Arginine
28
which CoFactors and coenzymes are necessary for amino acid metabolism?
```
Vitamin C
Vitamin B6
folic acid
iron
niacin
```
29
Which Amino acids disrupt secondary structures?
```
Proline
Glutamate
aspartate
histidine
lysine
arginine
tryptophan
valine
isoleucine
```
30
what are the two sulfur containing amino acids?
methionine
| cysteine
31
what is formed when two cysteine bind together?
sulfide bridge
32
why are serine and theronine important?
needed for phosphorylation to regulate protein
33
which amino acid is important in buffering?
histidine
34
why would cell recycling occur?
misfolding
damage by free radical or oxidation
not needed
35
explain the primary level of protein structure?
- sequence of amino acids
- includes covalent bonding
- sequence determines 2 and 3 sructures and acts as signals
36
explain the secondary level of protein structure?
stabilized by nonconvalent interactions (IMF)
alpha-helix
Beta pleated sheets
Beta- bends
most proteins have a mixture of 2 structures
37
explain the tertiary level of protein structure?
```
3-D arrangement
influenced by R-groups
Covalent bonds
-disulfide bonds
Noncovalent
-H.Bonds, ionic interactions, LDF
```
38
explain the quartenary level of protein structure?
```
Grouping of 2+ peptide chains
Noncovalent interactions (IMF)
H-bonds
ionic interactions
LDF
Hemogobin-4 peptide chains
alcohol dehydrogenase
```
39
which reaction mechanism is used in peptide bond formation?
condensation/dehydration
40
which pK is most important for the buffering capacity of proteins?
pKr
41
which IMF is important for stabilizing secondary structures?
Noncovalent interactions
| H-Bonds
42
Which amino acids are often found in beta-bonds?
proline
| glycine
43
which covalent interaction is involved in the tertiary structure?
Disulfide bonds
44
what do chaperone proteins help with?
they aid in protein folding.
- keep protein unfolded until synthesis is complete
- Act as catalysts for folding
- Prevent getting tangled during folding
45
how do heat, pH and mechanical shearing affect protein structure?
they unfold them
46
compare globular and fibrous proteins?
```
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
what holds oxygen in the heme structure?
Iron
48
where is myoglobin located?
muscles and heart
49
how many peptide chains does myoglobin have?
1
50
how many oxygens can myoglobin carry?
1
51
where is hemoglobin located?
red blood cells
52
how many peptide chains does hemoglobin have?
4
53
how many oxygens can hemoglobin carry?
4
54
compare R and T hemoglobin?
```
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
what is cooperative binding?
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
what effect will pH, CO2, CO, and 2,3-biphosphoglycerate have on hemoglobin?
will effect the heme to heme bonds
57
is the pH higher in the lungs or peripheral tissues?
| what does this mean for oxygen loading/unloading?
Lungs
58
under what conditions do we make 2,3 biphosphoglycerate?
concentration in RBC increases due to chronic hypoxia
59
how many polypeptides does collagen have?
3 polypeptides
60
which amino acids are found in the highest concentration in collagen?
proline
glycine
lysine
61
what is the difference between fibril-forming and network forming collagen?
which is found in higher concentrations in bone?
network forming is a 3D-mesh most common IV
| Fibril forming= rope like triple helix, common 1
62
what is the most common type of collagen in the human body?
type 1
63
what post-translational modification is important to the structure of collagen?
proline and vitamin C
Proline hydroxlase
post mod= functional group added after protein is synthesized
64
which coenzyme and cofactor are important in the posttransational modification?
vitamin C is the CoEnzyme
| Iron is the CoFactor
65
why is glycosylation important?
allows hydroxylysine to bind to glucose and galactose. some proteins do not fold correctly unless glycosylated first.
66
what does lysyl oxidase do? what is the cofactor for this reaction?
the CoFactor is Copper
- Deanimates lysine forming reactive aldehyde
- Aldehyde condenses with lysine or hydroxylysine on neighboring collagen
67
what are MMPs?
Matrix metalloproteinases
- main class of proteases
- Metallo= requires (Ca & Zn)
68
what pathways are MMPs involved in?
```
degenerative disc disease
inflammation
cancer
wound healing
osteoarthritis
atherosclerosis
rheumatoid arthritis
ulcers
endometriosis
```
69
where is elastin found?
found in the lungs
large arteries
and elastic ligaments
70
why might smoking be bad for the lungs?
smoking inhibits alpha1-antitrypsin (alpha1-AT), which is important for maintaining lung elasticity
71
what is a holoenzyme?
Complete (active) enzyme
72
what is a zymogen?
enzyme precursor (inactive enzyme)
73
identify cofactors?
inorganic component needed to work
Fe, Mg, Zn, Se
Minerals
74
identify CoEnzymes?
organic component needed to work
Vit. B6, Vit B12, thiamin, Folate, riboflavin, biotin, niacin
VITAMINS
75
identify the 6 classes of enzymes for a given reaction?
```
Oxidoreductase
transferase
isomerase
hydrolase
lyase
ligase
```
76
describe how enzymes speed up reactions?
they lower the activation energy
77
what kind of active site is the most common?
Induced-Fit Model
78
how do temperature and pH affect enzyme activity?
- 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
what are the other factors that affect enzyme activity?
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
describe how inhibitors affect Vmax and Km
S and I will compete for active site.
[S] will affect Km and Vmax
Inhibitors will affect Vmax only
81
determine which portion of the kinetics curve is dependent on substrate and/or enzyme concentration?
look at graph
82
what is the difference between a reversible and irreversible inhibitor?
```
Irreversible
-Covalent bonding
-Must make more enzyme to make product
Reversible
-Noncovalent interactions
Can dissociate
competitive
noncompetitive
```
83
what are allosteric enzymes?
-Regulatory enzymes in a cascade
| Rate-limiting
84
what is a negative and positive effector?
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
what is added/removed during covalent modification?
phosphate group to serine, theronine or tyrosine
86
what is enzyme induction?
- 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
describe protein digestion from mouth to excretion?location?
s
88
list the enzymes involved in protein digestion?Location?
s
89
list the secretions involved with protein digestion? location?
s
90
list the hormones involved in protein digestion?Location?
s
91
what is the difference between an exopeptidase and an endopeptidase?
s
92
how are the zymogens activated in the stomach and SI?
s
93
describe amoino acid and peptide absorption into the enterocyte?
s
94
How are the Amino acids transported across the basolateral membrane?
s
95
what is Apoenzyme?
protein part of enzyme only
