Exam 1 (lecture 6-9/16) Flashcards

(85 cards)

1
Q

List four functions of proteins

A
  1. Structural
  2. Movement and Localization of cells and molecules
  3. Ligand Binding
  4. Enzyme Catalysis
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2
Q

Structural proteins

A

gives cells their shape (usually fibrous)

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3
Q

Movement of cells and molecules proteins are broken up into:

A

Motor and membrane transport

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4
Q

Motor Proteins

A

cell movement, movement of chromosomes & organelles, causes change in conformations

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5
Q

Do motor proteins use ATP/GTP?

A

Yes. They use ATP/GTP hydrolysis to drive movement in one direction.

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6
Q

Membrane Transports

A

movement of molecules across the membrane, across entire membrane

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7
Q

Ligand

A

molecule bound by another proteins

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8
Q

Ligand Binding

A

protein folding creates a binding site. Ligand fits precisely into the binding site to maximize noncovalent interactions

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9
Q

More noncovalent interactions the more ______ to break apart

A

unlikely

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10
Q

What are the three types of protein-protein binding

A
  1. Surface-String
  2. Helix-Helix
  3. Surface-Surface
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11
Q

Antigen-Antibody Binding

A

tight, selective binding

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12
Q

Larger Ka

A

greater bonding strength (more products for assciation)

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13
Q

Larger Kd

A

not bound to eachother (lower affinty for eachother)

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14
Q

Equilibrium Constant

A

tells you if something prefers to be associated or not

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15
Q

if two proteins are known to bind the same ligand, this suggests….

A

proteins have similar structures

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16
Q

specificity of binding is determined by_______

A

a few amino acids near and within the binding site

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17
Q

Enzymes usually end in

A

-ase

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18
Q

Synthases

A

synthesize molecules in anabolic reactions by condensing two smaller molecules together

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19
Q

isomerases

A

catalyze the rearrangement of bonds within a single molecule

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20
Q

phosphatases

A

catalyze the hydrolytic removal of a phosphate group from a molecule

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21
Q

Pre-Steady State

A

ES (enzyme substrate) is just forming

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22
Q

Steady State

A

ES is almost constant, ES breaks downs and forms at the same rate

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23
Q

Steady State occurs when

A

there is enough substrate to saturate the enzyme and Vmax is achieved

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24
Q

K1

A

rate constant for formation for ES (association)

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25
K-1
rate constant for dissociation ES (dissociation)
26
Kcat
turnover number, rate constant equal to the number of substrate molecules processed per enzyme per second (# of substrate molecules that are produced per enzyme)
27
Michealis Constant (Km)
concentration of substrate needed for reaction to proceed at 0.5Vmax
28
Low Km= enzyme needs ____ substrate to be saturated
less
29
High Km= enzyme needs _____ substrate to be saturated
more
30
Catalytic efficiency
Kcat/Km
31
_______ can be used to compare the efficiency of two different enzymes or the efficiency of one enzyme with different substrates
catalytic efficiency
32
Activation Energy
energy required to reach the transition state (state of highest energy in rxn)
33
How do enzymes accelerate reactions?
1. increases the local reactant concentration 2. holds molecules in the correct orientation for the rxn 3. redistributes electrons to favor rxn 4. promotes or stabilizes the transition state
34
by promoting the transition state the enzyme needs to be
needs to be more complementary to transition site
35
What must be true of the reduction potential of electron carriers in the electron transport chain for the transfer of electrons to occur from one carrier to the next?
Each complex further along must have a higher reduction potential
36
High Reduction Potential=
Acceptor of Electrons
37
Low Reduction Potential=
Electron Donor
38
Complex 1:
``` Name: NADH Dehydrogenase Donor: NADH Acceptor: Ubiquinone (Q) How many H+ pumped: 4 How many e- can be carried: 1-2 ```
39
Complex 2
``` Name: Succinate Dehydrogenase Donor: FADH2 Acceptor: Ubiquinone How many H+ pumped: NONE How many e- can be carried: ```
40
Complex 3
``` Name: Cytochrome B-C1 Donor: Q Acceptor: Cytochrome C How many H+ pumped: 4 How many e- can be carried: 1 ```
41
Complex 4
``` Name: Cytochrome Oxidase Donor: Cytochrome C Acceptor: O2 How many H+ pumped: 2 How many e- can be carried: ```
42
Explain why 1 molecule of FADH2 is only capable of generating 2 ATP, while 1 molecule of NADH is capable of generating 3 ATP
FADH2 doesn't go through complex 1 . Transfering electrons from NADH there is a greater concentration gradient
43
alpha helices are not observed until the chain is at least 6 amino acids long. Why?
you need 5 to see the first interaction and with 6 you see 2 (think: N+4)
44
Ionic is
polar charged and can be acidic or basic
45
Acidic charged amino acids examples
Negative | Glu or Asp
46
Basic charged amino acids examples
Positive | His, Cys, Asn
47
Van der waals can have ____ amino acids interacting
any
48
Hydrogen bonding amino acids just need to be
POLAR! think: electronegative (N or O)
49
Large Ka or Small Kd favors
association
50
Large Kd or Small Ka favors
dissociation
51
Vmax
max velocity of a reaction for a given amount of an enzyme
52
In the steady state, the enzyme is likely to be bound so reaction goes close to _____
max velocity
53
Increase/High Kcat
more efficient enzyme
54
small Km equals ______ efficient
more
55
Best enzyme has a ____ Kcat and ____Km
Large Kcat and Small Km
56
What regulates enzymes?
Number of enzymes present, localization of enzymes to particular cellular compartments, modifications of enzymes to alter activity, inhibition by binding of an activator inhibitor
57
Negative Feedback
once enough of a product is produced it stops producing it
58
Competitive Inhibition
some inhibitor competes for the binding site where the substrate would normally bind; prevent the normal substrate to bind
59
Does competitive inhibition effect vmax?
No
60
Noncompetitive inhibition
inhibitor will bind to different site on the enzyme, substrate can still bind but it is unable to catalyze the reaction
61
What happens to Km in Noncompetitive inhibition?
Nothing--stays the same
62
What happens to vmax in noncpmpetitive inhibition?
it decreases. (Y changes on graph)
63
Allosteric Regulation
molecule binding to a seperate site on a regulatory subunit that results in a change in the subunit where the reaction occurs
64
Binding at one site affects the conformation of the second site
Allosteric Regulation
65
Positive Allosteric Regulation
when binding of one molecule increases the binding of a second molecule, these molecules are said to bind cooperatively.
66
Positive Allosteric Regulation occurs when both molecules prefer the ______ enzyme conformation.
same
67
Negative Allosteric Regulation
presence of one molecule interferes with binding of the second molecule
68
Negative Allosteric regulation occurs when both molecules prefer a ________ enzyme coformation
different
69
Aspartate Transcarbamoylase (ATCase) is an example of:
allosteric regulation
70
Aspartate Transcarbamoylase (ATCase) has how many regulatory and catalytic subuntis
3 of each
71
Aspartate Transcarbamoylase (ATCase) functions in production of:
pyrimidines (C, U, T)
72
Binding of substrates (asparatate and carbamoyl) shift to the R state is an example of:
Positive Allosteric Regulation
73
R state
Active state
74
T state
inactive state
75
CTP shifts to T state is an example of:
negative feedback inhibition
76
Modification of a protein by a phosphate group can?
increase or decease protein activity
77
Kinase
add phosphate group
78
Phosphatase
removes phosphate group
79
Src-type Kinase
regulated by multiple events; demonstrates the importance of enzymes being active only at the appropriate time and place
80
Modification of a protein by a phosphate group can:
increase or decrease protein activity
81
GTP is a:
nucleotriphosphate
82
When GTP is bound it is on the _____ state
on
83
When GTP is hydrolzyed to GDP it is in the _____ state
off
84
GEF (Guanine nucleotide exchange factor)
causes exchange of GDP for GTP (gets us to the active form)
85
GAP (GTPase activating protein)
induces hydolysis of GTP to GDP (gets us to the inactive form)