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HumBio 3A > MidTerm review > Flashcards

MidTerm review Flashcards

1
Q

<p>covalent bond</p>

A

<p>two atoms share electrons (valence electrons)</p>

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2
Q

<p>polar covalent bond</p>

A

<p>unequal sharing of electrons, causing partial ionic charge</p>

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3
Q

<p>non-polar covalent bond</p>

A

<p>equal/balanced sharing of electrons </p>

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4
Q

<p>ionic bond</p>

A

<p>electrostatic attraction between 2 oppositely charged ions - result of transfer of electrons from one atom to the other </p>

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5
Q

<p>anion</p>

A

<p>+electrons</p>

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6
Q

<p>cation</p>

A

<p>-electrons</p>

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7
Q

<p>4 major molecules in human body</p>

A

<p>carbohydrates, lipids, proteins, nucleaic acids

| </p>

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8
Q

<p>catabolism</p>

A

<p>glucose --> glycolysis or citric acid cycle</p>

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9
Q

<p>polar molecule</p>

A

<p>resulting from polar bonds, asymmetric electron sharing</p>

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10
Q

<p>types of cell energy</p>

A

<p>ATP, GTP, NADH, FADH2, pyruvate, acetyl coa</p>

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11
Q

<p>catabolism</p>

A

<p>energetically favorable reactions</p>

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12
Q

<p>anabolism</p>

A

<p>energetically unfavorable reaction</p>

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13
Q

<p>3 activities powered by ATP hydrolysis</p>

A

<p>pumping/transport
movement/mechanical
biosynthetic</p>

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14
Q

<p>catalysis</p>

A

<p>speeding a reaction by lowering the activation barrier</p>

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15
Q

<p>the hydrophobic portions of amino acids is typically found in/on the \_\_\_\_\_\_\_\_\_ of the conformation</p>

A

<p>inside</p>

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16
Q

<p>non-polar molecules are hydro\_\_\_\_\_\_\_</p>

A

<p>phobic</p>

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17
Q

<p>polar molecules are hydro\_\_\_\_\_\_\_</p>

A

<p>philic</p>

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18
Q

<p>Some enzymes require non-protein \_\_\_\_\_\_\_\_\_ for activity</p>

A

<p>cofactors</p>

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19
Q

<p>examples of co-factors</p>

A

<p>vitamins etc. </p>

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20
Q

<p>can the delta G from two reactions be added together</p>

A

<p>yes! if they're coupled</p>

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21
Q

<p>does delta G predict rate?</p>

A

<p>NO</p>

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22
Q

<p>what does delta G predict?</p>

A

<p>possibility/spontanaeity</p>

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23
Q

<p>a reactant makes a \_\_\_\_\_\_</p>

A

<p>product</p>

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24
Q

<p>a product is made from a \_\_\_\_\_\_</p>

A

<p>reactant</p>

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25
Q

<p>How do cells overcome the activation barrier for reactions?</p>

A

<p>a catalyst!!</p>

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26
Q

<p>A \_\_\_\_\_\_ helps cells overcome activation barriers</p>

A

<p>catalyst</p>

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27
Q

<p>is ATP stored?</p>

A

<p>no! it's continuously generated</p>

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28
Q

<p>what's an enzyme?</p>

A

<p>a highly specific catalyst</p>

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29
Q

<p>how do enzymes work?</p>

A

<p>they lower the activation energy of their substrate , catalyzing a reaction</p>

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30
Q

<p>3 ways an enzyme catalyzes (lowers activation barrier) of a substrate</p>

A

<p>1. binds 2 substrates and orients

2. binds and reorients electrons of 1 substrate
3. binds and strains / conforms 1 substrate to favorable transition state</p>

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31
Q

<p>How do enzymes maintain specificity?</p>

A

<p>they have unique structures and binding sites for subsrates</p>

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32
Q

<p>are enzymes and substrates bound by covalent bonds?</p>

A

<p>NO!

| </p>

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33
Q

<p>types of bonds that determine protein and enzyme structure:</p>

A

<p>electrostatic attractions
van der Waals attractions
hydrogen bond
</p>

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34
Q

<p>Enzymes can be \_\_\_\_\_\_\_ by molecules that resemble the substrate</p>

A

<p>inhibited</p>

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35
Q

<p>a molecule that resembles a substrate, and fills active/binding pocket without catalyzing a reaction is a \_\_\_\_\_\_\_\_\_\_</p>

A

<p>competitive inhibitor</p>

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36
Q

<p>providing \_\_\_\_\_\_ can be helpful for patients with methanol poisoning</p>

A

<p>ethanol</p>

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37
Q

<p>malonate \_\_\_\_\_\_\_ succinate hydrogenase by filling its active site and preventing the conversion of succinate to fumarate</p>

A

<p>inhibits</p>

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38
Q

<p>two types of catalytic enzyme inhibition</p>

A

<p>allosteric (regulatory site binding) and competitive (active site binding)</p>

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39
Q

<p>where does glycolysis take place?</p>

A

<p>cytoplasm</p>

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40
Q

<p>where does the CAC take place</p>

A

<p>the mitochondrial matrix</p>

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41
Q

<p>motif/scheme of signaling pathways</p>

A

<p>1. signal reception - on receptor, in or out

2. relay mechanism - pathway/cascade
3. downstream effects - on effector, what happens?</p>

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42
Q

roles of actin

A

muscle fibers
microvilli
projections (gut)

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43
Q

roles of microtubules

A 
mechanical support
cytoplasm organization
transport
motility - digestion
chromosomal segregation
44
Q

intermediate filaments

A

lamins

structural

45
Q

subunits of actin

A

G-actin monomer
F-actin fibers
Arp2/3 - nucleating/branch
formin - nucleating/head

46
Q

subunits of microtubules

A 
aB heterodimers
G turc
centrosome
GTP tubulin
GDP tubulin
cap of GTP tubulin
47
Q

_______ is hard, _________ is easy

A

nucleation, elongation

48
Q

intermediate filaments subunits

A

monomer
coiled-coil dimer
staggered tetramer
two tetramers

49
Q

intermediate filament polarity (micro/macro)

A

polar/ non-polar

50
Q

microtubule polarity (micro/macro)

A

polar/polar

51
Q

actin polarity (micro/macro)

A

polar/polar

52
Q

nucleating element of microtubules

A

G turc

53
Q

nucleating element of actin

A

formin and Arp2/3

54
Q

myosin walks on _______ in the ______ direction

A

actin , positive

55
Q

formin adds subunits to the _____ end, and then filament extends to the ______ direction, and grows to the ______ direction

A

positive, negative, negative?

56
Q

what causes dynamic instability?

A

the GTP tubulin dimers hydrolyze into GDP, and lose stability

57
Q

what are the benefits of dynamic instability?

A

“search and capture” mode, where they explore until they find their destination

58
Q

microtubule motor proteins and direction

A

dynine - negative

kinesin - positive

59
Q

dynine purpose

A

motor protein, carries vesicles etc., cilia, flagella

60
Q

kinesin purpose

A

motor protein, axonal transport etc.

61
Q

what role does actin play in mitosis?

A

the contractile ring

62
Q

what role do microtubules play in mitosis?

A

chromosomal organization

63
Q

myosin power stroke steps

A
  1. myosin bound to actin
  2. ATP binds to myosin, myosin releases
  3. ATP hydrolyzed, myosin returns to resting position
  4. cross bridge forms, and myosin head binds to new position on actin
  5. P released, myosin heads change conformation, causing power stroke, filaments slide past eachother
  6. ADP release, and myosin remains bound to actin.
64
Q

another name for H+

A

proton

65
Q

if you remove an electron from hydrogen, you get…

A

a proton

66
Q

H+ is purely____

A

acidic

67
Q

pH stands for ______

A

power of hydrogen

68
Q

pH of 7 is _____

A

neutral

69
Q

hexokinase

A

enzyme that catalyzes breakdown of glucose to glucose 6 phosphate

70
Q

substrates can bind through what bonds

A

ionic, hydrogen and covalent

71
Q

a catalyst will ______ a reaction

A

speed up

72
Q

does catalysis change delta G

A

no

73
Q

two factors that determine the rate of a reaction

A

activation energy and concentration

74
Q

an irreversible reaction has a _____ delta G going backwards

A

positive

75
Q

if a reaction is reversible, it’s likely that delta G is _________

A

very small

76
Q

reversible reactions generally proceed in the direction of _________

A

lower concentration

77
Q

Glycolysis input

A

glucose, 2 ATP, 2 NAD+

78
Q

Glycolysis output

A

2 pyruvate, 4 ATP, 2 NADH

79
Q

Glycolysis location

A

cytoplasm

80
Q

Fermentation input

A

2 pyruvate, 2 NADH

81
Q

Fermentation output

A

2 lactate, 2 NAD+

82
Q

Fermentation location

A

cytoplasm

83
Q

CAC input

A

acetyl CoA / oxaloacetate, FAD, GDP, 3 NAD+

84
Q

CAC output

A

3 NADH, 1 FADH2, 1 GTP, 2 Co2

85
Q

CAC location

A

matrix

86
Q

ETC input

A

NADH, FADH2 (electrons)

87
Q

ETC output

A

ATP, NAD+, FAD

88
Q

ETC location

A

inner mito. membrane

89
Q

Glucose carbon number

A

6

90
Q

Fructose 1,6 biphosphate carbon number

A

6

91
Q

G3P carbon number

A

3

92
Q

1,3 BPG carbon number

A

3

93
Q

pyruvate carbon number

A

3

94
Q

acetyl CoA carbon number

A

2

95
Q

oxaloacetate carbon number

A

4

96
Q

citrate carbon number

A

6

97
Q

ketogenesis

A

starvation response, triggered by glucagon

98
Q

does ketogenesis make the blood acidic?

A

YES! it releases ketones, which are acidic

99
Q

3-phosphoglycerate number of carbons

A

3

100
Q

citrate carbon number

A

6

101
Q

to get G3P molecules we______

A

isomerize

102
Q

citrate is made from _____ + ______`

A

acetyl CoA + oxaloacetate

103
Q

poly uria

A

excessive urination

104
Q

polydipsia

A

excessive thirst

105
Q

polyphagia

A

increased appetite

106
Q

are intermediate filaments polar

A

subunits yes, but not the macro

107
Q

hello

A

world

HumBio 3A (15 decks)

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