clicker questions exam iii Flashcards

1
Q

What is the difference between myoglobin and hemoglobin?

A

Myoglobin stores oxygen and hemoglobin transports it

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2
Q

The heme group, depending on the amino acid surrounding it, can bind:

A

Oxygen, co2, carbon monoxide

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3
Q

What is the p50 value of myoglobin

A

2.8 torr

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4
Q

What does the slope of the hill plot represent

A

cooperativity

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5
Q

What is the function of the protein surrounding the heme?

A

Modulates oxygen binding

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6
Q

Hemoglobin molecule contains how many Hemes?

A

4

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7
Q

What is the difference between the red and blue molecule shown?

A

Red- relaxed. r state, OXY
blue: constricted. t state, DEOXY

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8
Q

What is the structural reason for the bohr effect?

A

salt bridge which is lost in r state

Hydrogen binding at n term

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9
Q

Remembering the oxygen binding curves, a shift to the left represents?

A

Tighter binding of oxygen

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10
Q

How does BPG help in adapting hemoglobin to higher altitudes

A

Shifts the oxygen binding curve to the right

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11
Q

What is a structural reason for the BPG effect

A

binds to Beta hemoglobin

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12
Q

What effect does Boston mutation have on hemoglobin

A

Promotes methemoglobin formation

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13
Q

What is protein cooperativity?

A

How one binds compared to the next one binding.

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14
Q

How can cooperativity be measured?

A

Hill Equation

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15
Q

What happens to Ligand binding when there is a positive cooperativity

A

binding increases

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16
Q

What is the role of CA +2 in actin filament binding

A

binds to troponin, rotates, the actin so myosin head can bind to it

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17
Q

What causes the myosin power stroke?

A

Removing ADP

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18
Q

What is a similarity of myosin and kinesin movement

A

They both use ATP
They both move around

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19
Q

What is a difference between kinesin and myosin

A

Myosin comes in groups and is also actin. kinesin only has two heads that rotates and is microfilaments.

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20
Q

What is the role of an enzyme?

A

Speed up reaction

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21
Q

Specificity of an enzyme for a substrate is defined by

A

Active sites shape (amino acids), and complementary.

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22
Q

Define what a cofactor is

A

Another molecule that binds the protein and helps the reaction occur

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23
Q

In what way can enzymes be regulated?

A

Feedback inhibition
Allosteric regulation

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24
Q

What is DDGcat=/

A

Difference between activation energy with and without enzyme

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25
What do enzymes change in the energy graph?
Activation energy
26
What stays the same in the energy graph?
Delta G, reactant amount
27
What is the main attribute of an acid/base mechanism?
Proton exchange
28
What defines a covalent bonding mechanism
Chemical bond that is heavy
29
Metal ions can act as what during an enzymatic mechanism
Charge stabilization Ionization agent Shielding agent
30
Define proximity effect
Organization of substrates, closer together will react
31
Define a Mechanism transition state
Intermediate??
32
Which catalytic mechanism is defined by proton movement
Acid base catalyst
33
Which of these counts for no more than 5X effect on rate
Proximity effect
34
Which type of catalyst can use iron
Metal ion aided catalyst
35
What type of mechanism does lysozyme use?
Acid base
36
Why does lysozyme use acid base?
Acid base is major, there is a movement of proton
37
What determines the substrate of serine type protease
Specificity pocket
38
What is affinity labeling?
Trojan horse effect, binds pocket and then binds nearby acid amino acid
39
What catalytic mechanism do serine protease use?
Covalent bond catalysis
40
What kind of mechanism could ATP hydrolysis be classified as?
Acid base catalysis
41
What kind of reaction could ATP phosphorylation be classified as
Covalent bond catalysis
42
What is the role of Mg ++ in these reaction
It's stealing the charge, charge shielding
43
Kinetic data combined with ——- data allows the mechanism of a reaction to be determined
Structural
44
What is meant by order of a reaction
Number of molecules that must combine for reaction to occur
45
What is meant by the term half-life
Time it takes for half material to disappear
46
What order of reaction is half-life usually associated with
One
47
What does catalysis do to activation energy?
Lowers
48
The greater the delta G =/ the more —— the transition state is and the—— the reaction
Unstable, slower
49
How many fold is a reaction with DDG=/ cat of 17.13 kj/mol increased
1000
50
The following reaction 2A +B -> C represents which order of reaction
2
51
If an isotope has a half-life of 11 years, how many years have passed approximately 3.66% remains
55
52
What is the approximate k of an isotope if the half-life is 11 years?
.063/years
53
The determining step of a reaction with a stable intermediate, is the step with the: a. Highest DeltaG B. Smallest DG C. Highest. DDG D. Smallest DDG
Highest DG
54
What does DDG=/ represent
Change in activation energy
55
What is the main assumption of Michaelis-mentee eq.
Steady state
56
What is the difference between a equilibrium and steady state
Steady only forwards, equilibrium forward and backward.
57
What does Km represent?
Substrate concentration
58
What does Kcat/Km represent in enzymes
Catalytic efficiency
59
Why use lineWeaver- Burke instead of michaelis-menten
More accurate
60
When does enzymatic perfection occur?
When it is diffusion is limited.
61
Define random binding reactions
The order in which the substrate binding is random
62
Which type of competition has no change in Km
Noncompetitive
63
Which competition has the inhibitor binding at the substrate binding site
competitive
64
What is the effect of pH on an enzymes kinetics?
Change in Vmax and KM.