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BCHS > clicker questions exam iii > Flashcards

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
Q

What do enzymes change in the energy graph?

A

Activation energy

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26
Q

What stays the same in the energy graph?

A

Delta G, reactant amount

27
Q

What is the main attribute of an acid/base mechanism?

A

Proton exchange

28
Q

What defines a covalent bonding mechanism

A

Chemical bond that is heavy

29
Q

Metal ions can act as what during an enzymatic mechanism

A

Charge stabilization
Ionization agent
Shielding agent

30
Q

Define proximity effect

A

Organization of substrates, closer together will react

31
Q

Define a Mechanism transition state

A

Intermediate??

32
Q

Which catalytic mechanism is defined by proton movement

A

Acid base catalyst

33
Q

Which of these counts for no more than 5X effect on rate

A

Proximity effect

34
Q

Which type of catalyst can use iron

A

Metal ion aided catalyst

35
Q

What type of mechanism does lysozyme use?

A

Acid base

36
Q

Why does lysozyme use acid base?

A

Acid base is major, there is a movement of proton

37
Q

What determines the substrate of serine type protease

A

Specificity pocket

38
Q

What is affinity labeling?

A

Trojan horse effect, binds pocket and then binds nearby acid amino acid

39
Q

What catalytic mechanism do serine protease use?

A

Covalent bond catalysis

40
Q

What kind of mechanism could ATP hydrolysis be classified as?

A

Acid base catalysis

41
Q

What kind of reaction could ATP phosphorylation be classified as

A

Covalent bond catalysis

42
Q

What is the role of Mg ++ in these reaction

A

It’s stealing the charge, charge shielding

43
Q

Kinetic data combined with ——- data allows the mechanism of a reaction to be determined

A

Structural

44
Q

What is meant by order of a reaction

A

Number of molecules that must combine for reaction to occur

45
Q

What is meant by the term half-life

A

Time it takes for half material to disappear

46
Q

What order of reaction is half-life usually associated with

A

One

47
Q

What does catalysis do to activation energy?

A

Lowers

48
Q

The greater the delta G =/ the more —— the transition state is and the—— the reaction

A

Unstable, slower

49
Q

How many fold is a reaction with DDG=/ cat of 17.13 kj/mol increased

A

1000

50
Q

The following reaction 2A +B -> C represents which order of reaction

A

2

51
Q

If an isotope has a half-life of 11 years, how many years have passed approximately 3.66% remains

A

55

52
Q

What is the approximate k of an isotope if the half-life is 11 years?

A

.063/years

53
Q

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

A

Highest DG

54
Q

What does DDG=/ represent

A

Change in activation energy

55
Q

What is the main assumption of Michaelis-mentee eq.

A

Steady state

56
Q

What is the difference between a equilibrium and steady state

A

Steady only forwards, equilibrium forward and backward.

57
Q

What does Km represent?

A

Substrate concentration

58
Q

What does Kcat/Km represent in enzymes

A

Catalytic efficiency

59
Q

Why use lineWeaver- Burke instead of michaelis-menten

A

More accurate

60
Q

When does enzymatic perfection occur?

A

When it is diffusion is limited.

61
Q

Define random binding reactions

A

The order in which the substrate binding is random

62
Q

Which type of competition has no change in Km

A

Noncompetitive

63
Q

Which competition has the inhibitor binding at the substrate binding site

A

competitive

64
Q

What is the effect of pH on an enzymes kinetics?

A

Change in Vmax and KM.

BCHS (7 decks)

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