Motor Proteins (associated with actin filaments) Flashcards

(88 cards)

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
intrinsic ATPase activity resides in this myosin fragment
S1
26
actin binding ability resides in this myosin fragment
S1
27
S1 ATPase activity enhanced/activated by:
F-actin
28
these wrap around neck region and make it more rigid
light chains
29
type of skeletal muscle fibril can be immobilized on glass slide
myosin
30
end of actin that myosin "walks" to
+ end
31
actin is moved in direction of this charge on it
- end
32
using actin movement assay, these parts of myosin can move actin
HMM and S1
33
myosin domain determines cargo specificity
tail domain
34
part of myosin responsible for speed of actin filament movement
myosin neck
35
number of S1 myosin domains encoded in human genome
40 domains
36
these myosin families are widely distributed among eukaryotes
Myosin I, II, and V
37
all membrane associated actin filaments have this end pointed toward the plasma membrane
+ end
38
myosin class is the only with a single head
class I
39
myosin class binds specific receptors on organelles
Myosin V
40
myosin class involved in organelle transport
Myosin V
41
myosin class involved in membrane association and endocytosis
Class I
42
type of myosin is unique because it forms bipolar filaments
Myosin II
43
Myosin II coiled-coil tails interact with:
tails from other myosin molecules
44
part of Myosin II points outward from myosin bundles
myosin head
45
Myosin II bundle characteristic/property
bipolar "thick filaments"
46
myosin head bound tightly to actin when:
ATP is low
47
causes myosin to be released from actin filament
ATP binding
48
results in myosin head being in "cocked state"
ATP hydrolysis by myosin
49
myosin binding causes it to release this
Pi
50
caused by myosin head releasing Pi
"power stroke"
51
after power stroke the myosin head remains bound until release of:
ADP
52
light exerts this on matter
force
53
devise measure very small forces
optical trap
54
optical trap uses these three parts
laser beam, microscope, charged bead
55
optical trap charged bead attracted to:
intense light at center
56
optical trap: force applied to particle depends linearly on:
displacement from trap center
57
can be used to measure distance myosin molecules move actin filament each step
optical traps
58
optical trap experiment: force can be measured by determining:
how much beam has to be increased to keep filament in place
59
myosin type does not continuously interact with actin filaments
Myosin II
60
name describing myosin motor that does not continuously interact with actin filaments
non-processive motor
61
name describing myosin motor that does not release actin filament
processive motor
62
this myosin can make many sequential steps without releasing actin filament
Myyosin V
63
describes how long myosin is in contact with filaments for ATPase cycle
duty ratio
64
Duty Ratio of Myosin II
10%
65
Duty Radio of Myosin V
70%
66
myosin type produces optical trap graph produced does not have steps
Myosin II
67
myosin type releases ADP at slower rate
Myosin V
68
myosin type takes clear 36nm steps, one after another
Myosin V
69
each myosin V head moves this far
72 nm
70
myosin type moves "hand-over-hand"
myosin V
71
actin filament oriented with + end in:
Z disc
72
contraction brings myosin thick filament closer to this end of actin
+ end
73
actin filaments in sarcomere are stabilized at + end by:
CapZ
74
actin filaments in sarcomere are stabilized at - end by:
tropomodulin
75
protein extends along thin filament from Z-disc to tropomodulin
Nebulin
76
consists of actin binding repeats
Nebulin
77
length of Nebulin determines length of:
thin filaments
78
large molecule with head in Z-disc and extends to middle of thick filament
Titin
79
muscle contraction: action potential at neuromuscular junction travels down:
transverse tubule
80
muscle contraction: transverse tubule continuous with:
sarcolemma (PM)
81
muscle contraction: action potential triggers:
release of Ca2+
82
muscle contraction: Ca2+ released from:
sarcoplasmic reticulum
83
muscle contraction: Ca2+ induces change in long molecule strucng head to tail along thin filament
Tropomyosin (TM)
84
muscle contraction: protein associated with each Tropomyosin (TM)
Troponin (TN)
85
Troponin three subunits
TN-T, TN-I, TN-C
86
without Ca2+ this blocks myosin-actin interaction
Tropomyosin
87
Ca2+ binds to:
TN-C
88
binding Ca2+ to TN-C triggers:
movement of TM (exposing actin binding sites)