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CBIO3400 > Motor Proteins (associated with actin filaments) > Flashcards

Motor Proteins (associated with actin filaments) Flashcards

1
Q

makes muscles contract

A

myosin II

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2
Q

structure in skeletal muscle made of multiculeated cells

A

fibers

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3
Q

each cell from fibers contain a bundle of:

A

myofibrils

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4
Q

each myofibril contains thousands of contractile units called:

A

sarcomeres

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5
Q

links ECM to cytoskeleton in muscle cells

A

dystrophin glycoprotein complex

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6
Q

signaling molecule in skeletal muscle

A

NOS

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7
Q

muscle contraction increases levels of:

A

Ca2+

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8
Q

Ca2+ increase during muscle contraction activates:

A

NOS

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9
Q

activation of NOS in skeletal muscle produces:

A

NO

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10
Q

caused by NO diffusion to blood vessels

A

smooth muscle relaxation

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11
Q

relaxing smooth muscle causes increased:

A

blood flow to muscle tissue

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12
Q

label the parts of a sarcomere

A
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13
Q

thin actin filament charge type embedded in Z-disk

A

positive charge

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14
Q

consists of thin filaments

A

I-band

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15
Q

consists of bipolar myosin thick filaments

A

A-band

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16
Q

first molecular motor identified from skeletal muscle

A

Myosin II

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17
Q

this part located at myosin N-terminus

A

globular heads

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18
Q

myosin globular heads at N-terminus contain:

A

force generating machinery

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19
Q

myosin globular heads, light chains, and hinge region connected to:

A

coiled-coil of two alpha helices

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20
Q

approach to ID functional domains within a protein is to:

A

cleave into fragments site-specific proteases

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21
Q

cleaves myosin into two fragments (heavy- and light-mero-myosin)

A

Chymotrypsin

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22
Q

protease cleaves HMM (heavy-mero-myosin) into subfragment 1 (S1) and subfragment 2 (S2)

A

Papain

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23
Q

subfragment contains myosin head and neck regions

A

S1

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24
Q

these comprise the myosin tail

A

S2 and LMM

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25
Q

intrinsic ATPase activity resides in this myosin fragment

A

S1

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26
Q

actin binding ability resides in this myosin fragment

A

S1

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27
Q

S1 ATPase activity enhanced/activated by:

A

F-actin

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28
Q

these wrap around neck region and make it more rigid

A

light chains

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29
Q

type of skeletal muscle fibril can be immobilized on glass slide

A

myosin

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30
Q

end of actin that myosin “walks” to

A

+ end

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31
Q

actin is moved in direction of this charge on it

A
  • end
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32
Q

using actin movement assay, these parts of myosin can move actin

A

HMM and S1

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33
Q

myosin domain determines cargo specificity

A

tail domain

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34
Q

part of myosin responsible for speed of actin filament movement

A

myosin neck

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35
Q

number of S1 myosin domains encoded in human genome

A

40 domains

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36
Q

these myosin families are widely distributed among eukaryotes

A

Myosin I, II, and V

37
Q

all membrane associated actin filaments have this end pointed toward the plasma membrane

A

+ end

38
Q

myosin class is the only with a single head

A

class I

39
Q

myosin class binds specific receptors on organelles

A

Myosin V

40
Q

myosin class involved in organelle transport

A

Myosin V

41
Q

myosin class involved in membrane association and endocytosis

A

Class I

42
Q

type of myosin is unique because it forms bipolar filaments

A

Myosin II

43
Q

Myosin II coiled-coil tails interact with:

A

tails from other myosin molecules

44
Q

part of Myosin II points outward from myosin bundles

A

myosin head

45
Q

Myosin II bundle characteristic/property

A

bipolar “thick filaments”

46
Q

myosin head bound tightly to actin when:

A

ATP is low

47
Q

causes myosin to be released from actin filament

A

ATP binding

48
Q

results in myosin head being in “cocked state”

A

ATP hydrolysis by myosin

49
Q

myosin binding causes it to release this

A

Pi

50
Q

caused by myosin head releasing Pi

A

“power stroke”

51
Q

after power stroke the myosin head remains bound until release of:

A

ADP

52
Q

light exerts this on matter

A

force

53
Q

devise measure very small forces

A

optical trap

54
Q

optical trap uses these three parts

A

laser beam, microscope, charged bead

55
Q

optical trap charged bead attracted to:

A

intense light at center

56
Q

optical trap: force applied to particle depends linearly on:

A

displacement from trap center

57
Q

can be used to measure distance myosin molecules move actin filament each step

A

optical traps

58
Q

optical trap experiment: force can be measured by determining:

A

how much beam has to be increased to keep filament in place

59
Q

myosin type does not continuously interact with actin filaments

A

Myosin II

60
Q

name describing myosin motor that does not continuously interact with actin filaments

A

non-processive motor

61
Q

name describing myosin motor that does not release actin filament

A

processive motor

62
Q

this myosin can make many sequential steps without releasing actin filament

A

Myyosin V

63
Q

describes how long myosin is in contact with filaments for ATPase cycle

A

duty ratio

64
Q

Duty Ratio of Myosin II

A

10%

65
Q

Duty Radio of Myosin V

A

70%

66
Q

myosin type produces optical trap graph produced does not have steps

A

Myosin II

67
Q

myosin type releases ADP at slower rate

A

Myosin V

68
Q

myosin type takes clear 36nm steps, one after another

A

Myosin V

69
Q

each myosin V head moves this far

A

72 nm

70
Q

myosin type moves “hand-over-hand”

A

myosin V

71
Q

actin filament oriented with + end in:

A

Z disc

72
Q

contraction brings myosin thick filament closer to this end of actin

A

+ end

73
Q

actin filaments in sarcomere are stabilized at + end by:

A

CapZ

74
Q

actin filaments in sarcomere are stabilized at - end by:

A

tropomodulin

75
Q

protein extends along thin filament from Z-disc to tropomodulin

A

Nebulin

76
Q

consists of actin binding repeats

A

Nebulin

77
Q

length of Nebulin determines length of:

A

thin filaments

78
Q

large molecule with head in Z-disc and extends to middle of thick filament

A

Titin

79
Q

muscle contraction: action potential at neuromuscular junction travels down:

A

transverse tubule

80
Q

muscle contraction: transverse tubule continuous with:

A

sarcolemma (PM)

81
Q

muscle contraction: action potential triggers:

A

release of Ca2+

82
Q

muscle contraction: Ca2+ released from:

A

sarcoplasmic reticulum

83
Q

muscle contraction: Ca2+ induces change in long molecule strucng head to tail along thin filament

A

Tropomyosin (TM)

84
Q

muscle contraction: protein associated with each Tropomyosin (TM)

A

Troponin (TN)

85
Q

Troponin three subunits

A

TN-T, TN-I, TN-C

86
Q

without Ca2+ this blocks myosin-actin interaction

A

Tropomyosin

87
Q

Ca2+ binds to:

A

TN-C

88
Q

binding Ca2+ to TN-C triggers:

A

movement of TM (exposing actin binding sites)

CBIO3400 (8 decks)

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