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

Biochemistry: Proteins, Rxn Rates, Glycolysis Flashcards

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
Q

Collagen is an example of which type of tertiary structure?

A

Fibrous (not water soluble)

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26
Q

Which two amino acids will be found in the globular shape of a protein?

A

Leucine and valine

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27
Q

X-ray diffraction is the best way to analyze which level of protein structure?

A

Tertiary

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28
Q

Antibodies are made from what?

A

Plasma cells (mature B lymphocytes)

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29
Q

Which four amino acids have pyruvate as a precursor?

A

Al and Lucy Isolate Vallerie

Alanine, Leucine, Isoluecine Valine

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30
Q

Oxaloacetate is a precursor to aspartate which can further produce which amino acids?

A

All Lice Thrive on Meth

Asparagine, Lysine, Threonine, Methionine

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31
Q

Which amino acid is a precursor for Heme?

A

Glycine

Serine -> glycine -> heme

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32
Q

Which amino acid is a precursor for nitric oxide?

A

Arginine

Glutamate -> arginine -> NO

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33
Q

What is the predominant antibody in a primary exposure?

A

IgM

M is Made first

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34
Q

What is the most plentiful antibody?

A

IgG

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35
Q

Which antibody is most prominent in the gingiva?

A

IgG

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36
Q

Which antibody can cross the placenta?

A

IgG

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37
Q

Which antibody causes bacterial aggregation?

A

IgA

38
Q

Which antibody is found in secretions (mucous, tears, saliva, breast milk)?

A

IgA

39
Q

IgA inhibits pathogens from _________.

A

adhering to surfaces

40
Q

Which antibody binds to allergens triggering a histamine release?

A

IgE

Type 1 hypersensitivity

41
Q

Histamine is always found within which two cells?

A

Mast cells and basophils

42
Q

What types of symptoms would be seen upon first exposure with a type 1 hypersensitivity reaction?

A

No symptoms -> IgE would be made and bind to basophils to be ready if exposed again

43
Q

What leads to histamine release in Type 1 hypersensitivity reaction?

A

Antigen binds to IgE on surface of basophil -> Ca+ allowed into cell -> depolarization leads to histamine release

44
Q

What is the basic structure of collagen?

A

Three polypeptide alpha chains form Triple Helix

45
Q

What three compounds can hydroxylate proline and lysine?

A

Vitamin C, ferrous ions, and alpha-ketogluterate

46
Q

Where does hydroxylation of proline and lysine take place?

A

Rough ER

47
Q

Weakened connective tissue, poor wound healing, and bleeding of the gums are all symptoms of which disease?

A

Scurvy

Vitamin C deficiency

48
Q

________ is the longest known protein.

A

Tropocollagen

49
Q

Which collagen disease will cause a malar rash?

A

Lupus

Young females, attacks DNA, Malar rash

50
Q

What allows for elastin to be more flexible than other collagens?

A

No hydroxylysine and typically no hydroxyproline

51
Q

What do osteogenesis imperfecta and Ehler’s Danlos syndrome have in common?

A

Both effect type 1 collagen

52
Q

Which molecule concentration provides the best estimate of collagen present in a given tissue?

A

Hydroxyproline

53
Q

T/F: Carbon monoxide binds to heme groups irreversibly.

A

True

54
Q

What is significant about the iron in a heme group?

A

Must be in a ferrous/reduced state

55
Q

T/F: Most of the carbon dioxide carried through blood is via hemoglobin.

A

False

Bicarbonate

56
Q

________ comprise 90% of enamel proteins.

A

Amelogenins

57
Q

Which disease results in a thin hypoplastic enamel layer?

A

Amelogenesis imperfecta

58
Q

Which vitamin insufficiency will result in a hypoplastic enamel layer?

A

Vitamin A and Vitamin D

59
Q

What is Km?

A

The concentration of substrate needed to reach 1/2 of V max

60
Q

What will be the effect of competitive inhibition?

A

It will decrease binding affinity so Km will increase (need more substrate to overcome competition)

61
Q

T/F: Competitive inhibition causes a shift in which direction?

A

To the right

62
Q

What is the effect of non competitive inhibition?

A

No effect on Km, will decrease Vmax

Graph shifts down

63
Q

In a Lineweaver-Burke plot, an uninhibited reaction will have the same point on the y axis as a non competitive reaction.

A

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
Q

T/F: Allosteric ligands bind to the active site.

A

False

Bind away from the active site

65
Q

______ is an example of an allosteric ligand.

A

ATP

66
Q

T/F: ATP can be a substrate and an allosteric inhibitor.

A

True

67
Q

What does it mean if a reaction results in a negative change in G?

A

Energy is given off in the rxn

68
Q

T/F: Energy is released in an endergonic reaction which would have a negative change in G.

A

False

Energy released = exergonic = negative change in G

69
Q

What two thermodynamic parameters would lead to an exergonic reaction (-deltaG)?

A

Entropy (+deltaS) = lots of randomness

Enthalpy (-deltaH) = heat given off

70
Q

T/F: Enzymes have no effect on reaction equilibrium.

A

True

71
Q

T/F: When a molecule gains electrons it is oxidized.

A

False

Leo says Gerrr

Lose electrons oxidized

Gain electrons reduced

72
Q

What is the main role of NADPH?

A

Electron carrier in the pentose pathway shunt -> reduces molecules

73
Q

What is the main role of NADH/FADH?

A

Electron carriers in Krebs cycle etc. Oxidated to form ATP

74
Q

What is the definition of pH?

A

pH = -log(H)

H = concentration of protons

75
Q

T/F: pH + pOH = 14

A

True

76
Q

If H+ concentration is 10^-5 what will the pOH be?

A 
pH = 5
pOH = 9
77
Q

What is the major buffer when H+ ions are released inside the cell?

A

Dihydrogen phosphate

78
Q

What is the major buffer when H+ ions are released outside the cell?

A

Carbonic acid

79
Q

Why are proteins such good buffers?

A

They contain many different functional groups with different pKa values

80
Q

Describe the basis of the Henderson-Hasselbalch equation?

A

pH = pKa when the acid is half neutralized

pH = pKa + log (base/acid)

81
Q

Transamination and oxidative deamination are both examples of what process?

A

Protein metabolism

82
Q

Which three amino acids are not transaminated?

A

Lysine, serine, and threonine

83
Q

__________ is required as a coenzyme for transamination.

A

Vitamin B6

84
Q

Transaminases cleave the ________ from amino acids.

A

alpha amino nitrogen

85
Q

Which amino acid undergoes rapid oxidative deamination?

A

Glutamate

86
Q

What are the two results of oxidative deamination?

A

alpha ketoacids or amonia

87
Q

What is the major enzyme that does oxidative deamination?

A

Glutamate dehydrogenase

88
Q

What is the major method of metabolism for anaerobic and facultative anaerobic bacteria?

A

Glycolysis (Embden-Meyerhof pathway)

Does not require oxygen

89
Q

What is the alternative metabolism method used by some aerobic bacteria?

A

ENTNER–DOUDOROFF PATHWAY

90
Q

What byproduct of glycolysis is cariogenic?

A

Lactic acid

91
Q

Where does glycolysis occur?

A

In the cytosol

NBDE Part 1 (31 decks)

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