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Biol 3310 > C4 Protein > Flashcards

C4 Protein Flashcards

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
Q

nucleases

A

hydrolysis of nucleic acids (cleaves phosphodiester bonds)

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26
Q

proteases

A

hydrolysis of proteins (breakdown peptide bonds)

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27
Q

kinase

A

phosphate transfer

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28
Q

phosphatase

A

hydrolytic removal of phosphate

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29
Q

ATPases

A

hydrolyze ATP

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30
Q

Three ways in which enzymes lower activation energy

A

1) binds and orients two substrates to encourage reaction 2) rearrange electrons within substrate 3) strains substrate into transition state

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31
Q

factors affecting enzyme activity

A

temp, ph, substrate concentration, inhibitors/activators

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32
Q

[ES] x k_cat

A

V

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33
Q

michaelis-menton equation. V=?

A

V_max x ( [S] / ( [S] + K_m ) )

34
Q

Achieved when enzyme is saturated with substrate

A

V_max

35
Q

Reaction velocity when the substrate concentration is at the K_m

A

V_max / 2

36
Q

K_m =

A

(k_off + k_cat) / (k_on)

37
Q

Michaelis-menten plot is a plot of ? vs ?

A

concentration vs velocity

38
Q

lineweaver-burke plot is a plot of ? vs ?

A

1/concentration vs 1/velocity

39
Q

the x intercept of a lineweaver burke plot is equal to

A

-1/K_m

40
Q

the y intercept of a lineweaver burke plot is equal to

A

1/V_max

41
Q

slope of a lineweaver burke plot is equal to

A

K_m / V_max

42
Q

inhibitors that bind so tightly to an enzyme that they “kill” it

A

irreversible

43
Q

bind to active site or compete with the normal substrate

A

competitive inhibitors

44
Q

changes the conformation site of the enzyme and interferes with its ability to catalyze

A

noncompetitive inhibitor

45
Q

a competitive inhibitor reduces ?

A

k_on

46
Q

a noncompetitive inhibitor reduces ?

A

k_cat

47
Q

a ? inhibitor gives a new V_max

A

noncompetitive

48
Q

On a L-B plot, a ? inhibitor has a different x-intercept

A

competitive

49
Q

On a L-B plot, a ? inhibitor has a different y-intercept

A

noncompetitive

50
Q

A ? inhibitor requires more substrate to get to its original V_max

A

competitive

51
Q

Enzymes that undergo a conformational change between active and inactive forms

A

allosteric

52
Q

What effect do allosteric effectors have on allosteric enzymes

A

change equiibrium

53
Q

Are synthesized as inactive precursors that require modification

A

zymogens

54
Q

What usually modifies zymogens

A

proteolytic cleavage

55
Q

A common mechanism for turning a protein on or off

A

de/phosphorylation

56
Q

Act as molecular timers

A

GTP-binding proteins

57
Q

How do GTP-binding proteins act as molecular timers

A

after hydrolysis of GTP, a slow step occurs where GDP dissociates before another GTP can attach

58
Q

EF-Tu is an example of this kind of protein

A

GTP-binding

59
Q

Function of EF-Tu

A

binds tRNA to ribosome

60
Q

hydrolysis of EF-Tu (attaches/releases) it to/from tRNA

A

releases

61
Q

A non-nucleic acid infectious disease

A

PrP

62
Q

if it takes one second for a molecule to move 1um, how long does it take to travel 10um?

A

100 seconds

63
Q

how does an alpha helix form

A

NH of every peptide bond is H-bonded to the C=O of peptide bond located 4 AA’s away

64
Q

CAP small domain binds to ?

A

DNA

65
Q

CAP large domain binds to ?

A

cyclic AMP

66
Q

Serine protease family (3)

A

elastase, chymotrypsin, trypsin

67
Q

Proteins secreted by the cell to form gel-like matrix

A

Fibrous

68
Q

Three fibrous proteins

A

keratin, collagen, elastin

69
Q

collagen structure

A

triple helix

70
Q

elastin structure

A

covalently crosslinked

71
Q

keratin structure

A

coiled coil

72
Q

target of antibody called ?

A

antigen

73
Q

hexokinase add phosphate to ? but ignores ?

A

D-glucose, L-glucose

74
Q

model enzyme

A

lysozyme

75
Q

lysozyme function

A

severs polysaccharide chains of cell walls of bacteria

76
Q

rhodopsin

A

non protein component of a rhodopsin protein that detects light

77
Q

Three methods of enzyme control

A

production of enzyme. compartmentalization of enzyme. enzyme itself (inhibitors, temp, ph)

78
Q

Amount of enzymes phosphorylated at any one time

A

1/3

79
Q

set of covalent modifications a protein contains at any moment

A

regulatory protein code

80
Q

in vitro literally mean?

A

in glass

81
Q

in vivo literally means

A

in the living

82
Q

How is protein AA sequence determined

A

breaking polypeptide with selective proteases

Biol 3310 (20 decks)

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