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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

How do cells overcome the activation barrier for reactions?

a catalyst!!

26

A ______ helps cells overcome activation barriers

catalyst

27

is ATP stored?

no! it's continuously generated

28

what's an enzyme?

a highly specific catalyst

29

how do enzymes work?

they lower the activation energy of their substrate , catalyzing a reaction

30

3 ways an enzyme catalyzes (lowers activation barrier) of a substrate

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

31

How do enzymes maintain specificity?

they have unique structures and binding sites for subsrates

32

are enzymes and substrates bound by covalent bonds?

NO! |

33

types of bonds that determine protein and enzyme structure:

electrostatic attractions van der Waals attractions hydrogen bond

34

Enzymes can be _______ by molecules that resemble the substrate

inhibited

35

a molecule that resembles a substrate, and fills active/binding pocket without catalyzing a reaction is a __________

competitive inhibitor

36

providing ______ can be helpful for patients with methanol poisoning

ethanol

37

malonate _______ succinate hydrogenase by filling its active site and preventing the conversion of succinate to fumarate

inhibits

38

two types of catalytic enzyme inhibition

allosteric (regulatory site binding) and competitive (active site binding)

39

where does glycolysis take place?

cytoplasm

40

where does the CAC take place

the mitochondrial matrix

41

motif/scheme of signaling pathways

1. signal reception - on receptor, in or out 2. relay mechanism - pathway/cascade 3. downstream effects - on effector, what happens?

42
roles of actin
muscle fibers microvilli projections (gut)
43
roles of microtubules
``` mechanical support cytoplasm organization transport motility - digestion chromosomal segregation ```
44
intermediate filaments
lamins | structural
45
subunits of actin
G-actin monomer F-actin fibers Arp2/3 - nucleating/branch formin - nucleating/head
46
subunits of microtubules
``` aB heterodimers G turc centrosome GTP tubulin GDP tubulin cap of GTP tubulin ```
47
_______ is hard, _________ is easy
nucleation, elongation
48
intermediate filaments subunits
monomer coiled-coil dimer staggered tetramer two tetramers
49
intermediate filament polarity (micro/macro)
polar/ non-polar
50
microtubule polarity (micro/macro)
polar/polar
51
actin polarity (micro/macro)
polar/polar
52
nucleating element of microtubules
G turc
53
nucleating element of actin
formin and Arp2/3
54
myosin walks on _______ in the ______ direction
actin , positive
55
formin adds subunits to the _____ end, and then filament extends to the ______ direction, and grows to the ______ direction
positive, negative, negative?
56
what causes dynamic instability?
the GTP tubulin dimers hydrolyze into GDP, and lose stability
57
what are the benefits of dynamic instability?
"search and capture" mode, where they explore until they find their destination
58
microtubule motor proteins and direction
dynine - negative | kinesin - positive
59
dynine purpose
motor protein, carries vesicles etc., cilia, flagella
60
kinesin purpose
motor protein, axonal transport etc.
61
what role does actin play in mitosis?
the contractile ring
62
what role do microtubules play in mitosis?
chromosomal organization
63
myosin power stroke steps
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
another name for H+
proton
65
if you remove an electron from hydrogen, you get...
a proton
66
H+ is purely____
acidic
67
pH stands for ______
power of hydrogen
68
pH of 7 is _____
neutral
69
hexokinase
enzyme that catalyzes breakdown of glucose to glucose 6 phosphate
70
substrates can bind through what bonds
ionic, hydrogen and covalent
71
a catalyst will ______ a reaction
speed up
72
does catalysis change delta G
no
73
two factors that determine the rate of a reaction
activation energy and concentration
74
an irreversible reaction has a _____ delta G going backwards
positive
75
if a reaction is reversible, it's likely that delta G is _________
very small
76
reversible reactions generally proceed in the direction of _________
lower concentration
77
Glycolysis input
glucose, 2 ATP, 2 NAD+
78
Glycolysis output
2 pyruvate, 4 ATP, 2 NADH
79
Glycolysis location
cytoplasm
80
Fermentation input
2 pyruvate, 2 NADH
81
Fermentation output
2 lactate, 2 NAD+
82
Fermentation location
cytoplasm
83
CAC input
acetyl CoA / oxaloacetate, FAD, GDP, 3 NAD+
84
CAC output
3 NADH, 1 FADH2, 1 GTP, 2 Co2
85
CAC location
matrix
86
ETC input
NADH, FADH2 (electrons)
87
ETC output
ATP, NAD+, FAD
88
ETC location
inner mito. membrane
89
Glucose carbon number
6
90
Fructose 1,6 biphosphate carbon number
6
91
G3P carbon number
3
92
1,3 BPG carbon number
3
93
pyruvate carbon number
3
94
acetyl CoA carbon number
2
95
oxaloacetate carbon number
4
96
citrate carbon number
6
97
ketogenesis
starvation response, triggered by glucagon
98
does ketogenesis make the blood acidic?
YES! it releases ketones, which are acidic
99
3-phosphoglycerate number of carbons
3
100
citrate carbon number
6
101
to get G3P molecules we______
isomerize
102
citrate is made from _____ + ______`
acetyl CoA + oxaloacetate
103
poly uria
excessive urination
104
polydipsia
excessive thirst
105
polyphagia
increased appetite
106
are intermediate filaments polar
subunits yes, but not the macro
107
hello
world

HumBio 3A (15 decks)

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