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Biol 3310 > C4 Protein > Flashcards

C4 Protein Flashcards

(82 cards)

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1
Q

Catalyzes formation or breakage of covalent bonds

A

Enzyme

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2
Q

Binds to DNA to switch genes on or off

A

Gene regulatory protein

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3
Q

Generates movement in cells and tissues

A

Motor protein

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4
Q

Used by cells to detect signals and transmit them to the cell’s response machinery

A

Receptor protein

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5
Q

Each succesive amino acid adds to the ? end of a peptide

A

carboxyl

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6
Q

Primary structure of protein?

A

amino acid sequence

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7
Q

Bond between amino acids in a protein

A

peptide

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8
Q

alpha-helix and beta-sheets are (1,2,3*) structures of Proteins

A

2*

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9
Q

Denatured protein in water using urea. Then observed conformation reformed upon removal of urea.

A

Anfrinson

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10
Q

Anfrinson determined..

A

amino acid sequence determines structure

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11
Q

The CAP protein has one large, and one small ?

A

domain

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12
Q

Any segment of a polypeptide chain that can fold independently into a compact, stable structure

A

domain

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13
Q

The secondary structure of proteins is generally a result of ?

A

H-bonding

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14
Q

The tertiary structure of proteins is a result of ?

A

side chain interactions

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15
Q

proteins with similar structure but different function

A

protein families

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16
Q

proteins made of four subunits

A

tetramer

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17
Q

dimer of the same two polypeptides

A

homodimer

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18
Q

hemoglobin is a dimer of ?

A

heterodimers

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19
Q

Simple, elongated, three-dimensinal protein

A

fibrous

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20
Q

myosin has this structure

A

coiled coil

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21
Q

Proteins bind their ? with great specificity

A

ligands

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22
Q

What is meant by high affinity binding?

A

The ligand with a higher affinity will be present in the binding region more readily than one with a low affinity

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23
Q

Enzyme binds to ? of substrate

A

transition state

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24
Q

hydrolases

A

catalyze hydrolytic cleavage

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25
nucleases
hydrolysis of nucleic acids (cleaves phosphodiester bonds)
26
proteases
hydrolysis of proteins (breakdown peptide bonds)
27
kinase
phosphate transfer
28
phosphatase
hydrolytic removal of phosphate
29
ATPases
hydrolyze ATP
30
Three ways in which enzymes lower activation energy
1) binds and orients two substrates to encourage reaction 2) rearrange electrons within substrate 3) strains substrate into transition state
31
factors affecting enzyme activity
temp, ph, substrate concentration, inhibitors/activators
32
[ES] x k_cat
V
33
michaelis-menton equation. V=?
V_max x ( [S] / ( [S] + K_m ) )
34
Achieved when enzyme is saturated with substrate
V_max
35
Reaction velocity when the substrate concentration is at the K_m
V_max / 2
36
K_m =
(k_off + k_cat) / (k_on)
37
Michaelis-menten plot is a plot of ? vs ?
concentration vs velocity
38
lineweaver-burke plot is a plot of ? vs ?
1/concentration vs 1/velocity
39
the x intercept of a lineweaver burke plot is equal to
-1/K_m
40
the y intercept of a lineweaver burke plot is equal to
1/V_max
41
slope of a lineweaver burke plot is equal to
K_m / V_max
42
inhibitors that bind so tightly to an enzyme that they "kill" it
irreversible
43
bind to active site or compete with the normal substrate
competitive inhibitors
44
changes the conformation site of the enzyme and interferes with its ability to catalyze
noncompetitive inhibitor
45
a competitive inhibitor reduces ?
k_on
46
a noncompetitive inhibitor reduces ?
k_cat
47
a ? inhibitor gives a new V_max
noncompetitive
48
On a L-B plot, a ? inhibitor has a different x-intercept
competitive
49
On a L-B plot, a ? inhibitor has a different y-intercept
noncompetitive
50
A ? inhibitor requires more substrate to get to its original V_max
competitive
51
Enzymes that undergo a conformational change between active and inactive forms
allosteric
52
What effect do allosteric effectors have on allosteric enzymes
change equiibrium
53
Are synthesized as inactive precursors that require modification
zymogens
54
What usually modifies zymogens
proteolytic cleavage
55
A common mechanism for turning a protein on or off
de/phosphorylation
56
Act as molecular timers
GTP-binding proteins
57
How do GTP-binding proteins act as molecular timers
after hydrolysis of GTP, a slow step occurs where GDP dissociates before another GTP can attach
58
EF-Tu is an example of this kind of protein
GTP-binding
59
Function of EF-Tu
binds tRNA to ribosome
60
hydrolysis of EF-Tu (attaches/releases) it to/from tRNA
releases
61
A non-nucleic acid infectious disease
PrP
62
if it takes one second for a molecule to move 1um, how long does it take to travel 10um?
100 seconds
63
how does an alpha helix form
NH of every peptide bond is H-bonded to the C=O of peptide bond located 4 AA's away
64
CAP small domain binds to ?
DNA
65
CAP large domain binds to ?
cyclic AMP
66
Serine protease family (3)
elastase, chymotrypsin, trypsin
67
Proteins secreted by the cell to form gel-like matrix
Fibrous
68
Three fibrous proteins
keratin, collagen, elastin
69
collagen structure
triple helix
70
elastin structure
covalently crosslinked
71
keratin structure
coiled coil
72
target of antibody called ?
antigen
73
hexokinase add phosphate to ? but ignores ?
D-glucose, L-glucose
74
model enzyme
lysozyme
75
lysozyme function
severs polysaccharide chains of cell walls of bacteria
76
rhodopsin
non protein component of a rhodopsin protein that detects light
77
Three methods of enzyme control
production of enzyme. compartmentalization of enzyme. enzyme itself (inhibitors, temp, ph)
78
Amount of enzymes phosphorylated at any one time
1/3
79
set of covalent modifications a protein contains at any moment
regulatory protein code
80
in vitro literally mean?
in glass
81
in vivo literally means
in the living
82
How is protein AA sequence determined
breaking polypeptide with selective proteases

Biol 3310 (20 decks)

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