Lecture 6 Flashcards

1
Q

the function of nearly all proteins depend on their ability to bind to molecules (ligands or substrates) with a

A

high degree of specificity

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2
Q

region of a protein that associates with a ligand

A

binding ste

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3
Q

protein-ligand interaction is mediated by

A

noncovalent bonds

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4
Q

protein-ligand interaction can be measured by

A

velocity, affinity (binding strength), and specificity (binding preference)

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5
Q

level of affinity and specificity depends on –

A

molecular complementaries

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6
Q

– identify crucial ligand-binding sites

A

evolutionary tracing method

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7
Q

most common way two proteins bind with each other

A

surface-surface

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8
Q

antibodies can directly – or mark it for destruction

A

inactivate target protein

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9
Q

T/F: antibodies can distinguish between proteins that differ by only one AA

A

true

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10
Q

foreign substance that elicits production of an antibody

A

antigen

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11
Q

subunits/polypeptides of an antibody

A

2 heavy chains and 2 light chains

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12
Q

the chains of an antibody are held together by

A

disulfide bonds

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13
Q

each polypeptide chain of an antibody can be divided into 2 domains

A

variable and constant

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14
Q

the – domains interact with the antigen

A

variable

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15
Q

ligand binding site in antibodies

A

hypervariable loop

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16
Q

interaction between antibody and epitope of antigen is

A

complementary

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17
Q

enzymes binds 2 molecules and – them to encourage a reaction to occur between them

A

precisely orients

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18
Q

binding of substrate to enzyme rearranges electrons in the substrate that –

A

favor a reaction

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19
Q

enzymes strains the bound substrate molecule, forcing it toward a – to favor a reaction

A

transition state

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20
Q

enzyme that catalyze a hydrolytic cleavage

A

hydrolase

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21
Q

break down nucleic acids by hydrolyzing bonds between nucleotides

A

nucleases

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22
Q

break down proteins by hydrolyzing bonds between AA

A

proteases

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23
Q

synthesize molecules in anabolic reactions by condensing two smaller molecules together

A

synthase

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24
Q

join together two molecules in an energy-dependent process

A

ligase

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25
catalyze rearrangement of bonds within a single molecule
iosmerase
26
catalyze polymerization reactions such as synthesis of DNA and RNA
polymerases
27
catalyze the addition of phosphate groups to molecules
kinases
28
hydrolyze ATP
ATPases
29
GTPase
hydrolyze GTP
30
dissociation rate
Koff * [AB]
31
association rate
Kon * [A][B]
32
dissociation rate = association rate at
equilibrium
33
Vmax
all enzymes are used
34
Km
substrate concentration at 0.5 Vmax
35
low Km
enzyme binds to substrate very tightly
36
enzyme's active site is made up of
catalytic site and binding pocket
37
trypsin-like serene proteases' catalytic site
serine, histidine, aspartate, oxyanion hole
38
trypsin-like serene proteases' catalytic site - serine
break peptide bond
39
trypsin-like serene proteases' catalytic site - histidine
stabilize (accept proton)
40
trypsin-like serene proteases' catalytic site - aspartate
orient histidine at right location by H bonding
41
trypsin-like serene proteases' catalytic site - oxyanion hole
stabilize intermediates
42
trypsin-like serene proteases' catalytic site - the binding site
is general
43
trypsin-like serine proteases' catalytic site - has a -- binding pocket
side chain specificity
44
Trypsin (Asp)
Arg and Lys (positive side chains)
45
Chymotrypsin (Ser)
Phe, Tyr, Trp (large hydrophobic side chains)
46
Elastase (Val)
Gly and Ala (small side chains)
47
substrate of lysozyme
6-sugar oligosaccharide
48
lysozyme breaks uses -- to break between the 4th and 5th sugar
glutamate and aspartate
49
final products of lysozyme are
4-sugar oligosaccharide and a disaccharide
50
proteins often use -- to carry functions that would be difficult using AA alone
small non-protein molecules
51
change conformation --> change function examples
allosteric walking and ABC transporter
52
enzymes in a common pathway are often --
physically associated with one another
53
-- hold related enzymes
scaffold
54
regulation of protein activity by kinase/phosphatase switch is an example of -- protein modification
covalent
55
T/F: kinase can only turn on proteins
false
56
Which amino acids are used in the kinase/phosphatase switch?
serine, threonine, tyrosine (hydroxyl group)
57
receptro tyrosine kinase is activated by --
dimerization
58
once RTK is active, they --
phosphorylate each other
59
Src-type kinase as --
signal-integrating device
60
refers to the changes of protein conformation and activity upon binding to a ligand
allosteric regulation
61
allosteric regulation is an example of -- protein modification
noncovalent
62
T/F: allosteric regulation can be positive or negative
true
63
active PKA has lost its
catalytic site
64
in allosteric regulation, the activity of an enzyme is either inhibited to activated by a regulatory molecule that binds to the allosteric site that is -- from the active site
distinct
65
the binding to the allosteric site produces a -- of the active site either simulating or inhibiting the enzyme to catalyze a reaction
conformational change
66
the binding of tryptophan changes the conformation of the --
repressor
67
allosteric switch of calmodulin is
noncovalent
68
GTP bound
ON
69
GDP bound
OFF
70
GAP (GTPases Activating Protein)
help turn off faster
71
GEF (Guanine Exchange Factor)
help turn on faster
72
when the amount of the -- is high it inhibits an enzyme that functions early in the reaction pathway
end product
73
three conformations of the acetylcholine receptor
unoccupied and closed occupied and open occupied and closed
74
most stable form of the acetylcholine receptor
occupied and closed (inactivated)
75
tryptophan repressor is an examples of -- modification
noncovalent
76
when there's a lot of tryptophan, it will bind to the -- which binds to the DNA and turns it off
tryptophan repressor
77
enzymatic cleavage of a backbone peptide bond, resulting in the removal of residues from the polypeptide chain
proteolytic cleavage
78
proteolytic cleavage is a common mechanism for activating enzymes that function in
programmed cell death
79
proteolysis also generates active peptide hormones such as -- from larger precursor polypeptides
insulin
80
proteolytic cleavage -- inactivates or activates proteins
irreversibly
81
Ubiquitin is a -- amino acid polypeptide that marks proteins for degradation
76
82
ubiquitin can be covalently linked to other proteins via a covalent bonds between an internal -- and its C-terminal
lysine on the substrate protein
83
monoubiquitylation
histone regulation
84
multiubiquitylation
endocytosis
85
polyubiquitylation (Lys 48)
proteosomal degradation
86
polyubiquitylation (Lys 63)
DNA repair
87
ubiquitin activating enzyme (E1) uses -- to attach ubiquitin to itself via a high energy thioester bond
ATP hydrolysis
88
E1 passes activated ubiquitin to --
E2 ubiquitin-conjugating enzymes
89
E2 works with E3 (ubiquitin ligases) which has the -- for the target protein
binding site