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NBDE Part 1 > Biochemistry: Proteins, Rxn Rates, Glycolysis > Flashcards

Biochemistry: Proteins, Rxn Rates, Glycolysis Flashcards

(91 cards)

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1
Q

What is the role of the rER?

A

Pump out generalized proteins

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2
Q

What is the role of the Golgi?

A

Make proteins specialized

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3
Q

What organelle produces steroids in the adrenal cortex?

A

Smooth ER

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4
Q

T/F: The mitochondria have a double membrane bilayer.

A

True

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5
Q

Which organelle contains its own cyclic DNA passed down from mothers?

A

Mitochondria

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6
Q

What enzyme is often involved in the production of cAMP?

A

Adenylyl cyclase

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7
Q

Alpha2, Beta1, and Beta2 receptors all work by modifying what enzyme?

A

Adenylyl cyclase

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8
Q

Amino acids are bound by what type of bonds?

A

Covalent bonds (strongest)

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9
Q

T/F: Electrostatic interactions are examples of covalent bonds.

A

False

Electrostatic, hydrogen, and van der waals are all noncovalent bonds

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10
Q

The amino acids in proteins are linked covalently by _________.

A

peptide bonds (amine bonds)

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11
Q

Aspartate can be broken down into ________.

A

oxaloacetate

*think ketone bodies

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12
Q

What is the precursor to tyrosine?

A

Phenylalanine

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13
Q

Melanin, dopamine, epinephrine, and norepinephrine can all be made through ________.

A

tyrosine

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14
Q

T/F: Lipids, carbohydrates and proteins all contain nitrogen.

A

False

Just proteins

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15
Q

T/F: Which amino acid is the precursor to serotonin?

A

Tryptophan

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16
Q

Decarboxylation of histidine leads to which vasodilator?

A

Histamine

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17
Q

T/F: Histamine is a vasodilator.

A

True

Dilate vessels, constrict lungs

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18
Q

Which amino acid is a precursor for GABA?

A

Glutamate

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19
Q

What is the basic protein structure?

A

Alpha carbon surrounded by four groups:

  1. Hydrogen
  2. Carboxyl
  3. Amino (Nitrogen)
  4. R group
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20
Q

T/F: All amino acids are in the L-configuration.

A

True

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21
Q

Which disease is linked to the incomplete metabolism of tyrosine?

A

Albinism

Deficiency in tyrosinase does not make enough melanin

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22
Q

T/F: The secondary structure of proteins is mediated by covalent bonds.

A

False

Alpha helicies, beta sheets, random coils

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23
Q

T/F: Tertiary structure is the three dimensional shape of the protein.

A

True

Globular and fibrous

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24
Q

Albumin is an example of which type of tertiary structure?

A

Globular (water soluble)

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25
Collagen is an example of which type of tertiary structure?
Fibrous (not water soluble)
26
Which two amino acids will be found in the globular shape of a protein?
Leucine and valine
27
X-ray diffraction is the best way to analyze which level of protein structure?
Tertiary
28
Antibodies are made from what?
Plasma cells (mature B lymphocytes)
29
Which four amino acids have pyruvate as a precursor?
Al and Lucy Isolate Vallerie Alanine, Leucine, Isoluecine Valine
30
Oxaloacetate is a precursor to aspartate which can further produce which amino acids?
All Lice Thrive on Meth Asparagine, Lysine, Threonine, Methionine
31
Which amino acid is a precursor for Heme?
Glycine Serine -> glycine -> heme
32
Which amino acid is a precursor for nitric oxide?
Arginine Glutamate -> arginine -> NO
33
What is the predominant antibody in a primary exposure?
IgM M is Made first
34
What is the most plentiful antibody?
IgG
35
Which antibody is most prominent in the gingiva?
IgG
36
Which antibody can cross the placenta?
IgG
37
Which antibody causes bacterial aggregation?
IgA
38
Which antibody is found in secretions (mucous, tears, saliva, breast milk)?
IgA
39
IgA inhibits pathogens from _________.
adhering to surfaces
40
Which antibody binds to allergens triggering a histamine release?
IgE Type 1 hypersensitivity
41
Histamine is always found within which two cells?
Mast cells and basophils
42
What types of symptoms would be seen upon first exposure with a type 1 hypersensitivity reaction?
No symptoms -> IgE would be made and bind to basophils to be ready if exposed again
43
What leads to histamine release in Type 1 hypersensitivity reaction?
Antigen binds to IgE on surface of basophil -> Ca+ allowed into cell -> depolarization leads to histamine release
44
What is the basic structure of collagen?
Three polypeptide alpha chains form Triple Helix
45
What three compounds can hydroxylate proline and lysine?
Vitamin C, ferrous ions, and alpha-ketogluterate
46
Where does hydroxylation of proline and lysine take place?
Rough ER
47
Weakened connective tissue, poor wound healing, and bleeding of the gums are all symptoms of which disease?
Scurvy Vitamin C deficiency
48
________ is the longest known protein.
Tropocollagen
49
Which collagen disease will cause a malar rash?
Lupus Young females, attacks DNA, Malar rash
50
What allows for elastin to be more flexible than other collagens?
No hydroxylysine and typically no hydroxyproline
51
What do osteogenesis imperfecta and Ehler's Danlos syndrome have in common?
Both effect type 1 collagen
52
Which molecule concentration provides the best estimate of collagen present in a given tissue?
Hydroxyproline
53
T/F: Carbon monoxide binds to heme groups irreversibly.
True
54
What is significant about the iron in a heme group?
Must be in a ferrous/reduced state
55
T/F: Most of the carbon dioxide carried through blood is via hemoglobin.
False Bicarbonate
56
________ comprise 90% of enamel proteins.
Amelogenins
57
Which disease results in a thin hypoplastic enamel layer?
Amelogenesis imperfecta
58
Which vitamin insufficiency will result in a hypoplastic enamel layer?
Vitamin A and Vitamin D
59
What is Km?
The concentration of substrate needed to reach 1/2 of V max
60
What will be the effect of competitive inhibition?
It will decrease binding affinity so Km will increase (need more substrate to overcome competition)
61
T/F: Competitive inhibition causes a shift in which direction?
To the right
62
What is the effect of non competitive inhibition?
No effect on Km, will decrease Vmax Graph shifts down
63
In a Lineweaver-Burke plot, an uninhibited reaction will have the same point on the y axis as a non competitive reaction.
False 1/velocity is represented on the Y axis so competitive and uninhibited will share point on y axis, non competitive will shift up
64
T/F: Allosteric ligands bind to the active site.
False Bind away from the active site
65
______ is an example of an allosteric ligand.
ATP
66
T/F: ATP can be a substrate and an allosteric inhibitor.
True
67
What does it mean if a reaction results in a negative change in G?
Energy is given off in the rxn
68
T/F: Energy is released in an endergonic reaction which would have a negative change in G.
False Energy released = exergonic = negative change in G
69
What two thermodynamic parameters would lead to an exergonic reaction (-deltaG)?
Entropy (+deltaS) = lots of randomness Enthalpy (-deltaH) = heat given off
70
T/F: Enzymes have no effect on reaction equilibrium.
True
71
T/F: When a molecule gains electrons it is oxidized.
False Leo says Gerrr Lose electrons oxidized Gain electrons reduced
72
What is the main role of NADPH?
Electron carrier in the pentose pathway shunt -> reduces molecules
73
What is the main role of NADH/FADH?
Electron carriers in Krebs cycle etc. Oxidated to form ATP
74
What is the definition of pH?
pH = -log(H) H = concentration of protons
75
T/F: pH + pOH = 14
True
76
If H+ concentration is 10^-5 what will the pOH be?
``` pH = 5 pOH = 9 ```
77
What is the major buffer when H+ ions are released inside the cell?
Dihydrogen phosphate
78
What is the major buffer when H+ ions are released outside the cell?
Carbonic acid
79
Why are proteins such good buffers?
They contain many different functional groups with different pKa values
80
Describe the basis of the Henderson-Hasselbalch equation?
pH = pKa when the acid is half neutralized pH = pKa + log (base/acid)
81
Transamination and oxidative deamination are both examples of what process?
Protein metabolism
82
Which three amino acids are not transaminated?
Lysine, serine, and threonine
83
__________ is required as a coenzyme for transamination.
Vitamin B6
84
Transaminases cleave the ________ from amino acids.
alpha amino nitrogen
85
Which amino acid undergoes rapid oxidative deamination?
Glutamate
86
What are the two results of oxidative deamination?
alpha ketoacids or amonia
87
What is the major enzyme that does oxidative deamination?
Glutamate dehydrogenase
88
What is the major method of metabolism for anaerobic and facultative anaerobic bacteria?
Glycolysis (Embden-Meyerhof pathway) Does not require oxygen
89
What is the alternative metabolism method used by some aerobic bacteria?
ENTNER–DOUDOROFF PATHWAY
90
What byproduct of glycolysis is cariogenic?
Lactic acid
91
Where does glycolysis occur?
In the cytosol

NBDE Part 1 (31 decks)

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