Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin
Author
Chalovich, Joseph; Johnson, Dylan
Abstract
Keywords: troponin, tropomyosin, cardiomyopathy, troponin T, mutations
Troponin-tropomyosin inhibits skeletal and cardiac muscle contraction at low Ca
rigor-type myosin S1 to actin-tropomyosin-troponin, particularly at saturating Ca2+, produces activation of myosin ATPase activity in excess of that seen in the absence of the regulatory proteins. The binding energy of S1 can overcome the inhibitory activity of troponin (Bremel et al., 1972) and may allow tropomyosin to move deep into the groove of actin. That particular arrangement of actin, tropomyosin, and troponin is a much better activator of ATP hydrolysis than actin alone. That active configuration of actin was called state 2 in the Hill model (Hill et al., 1980) and later named the M state because of its requirement for tight myosin binding.
Date
2016-08-31
Citation:
APA:
Chalovich, Joseph, & Johnson, Dylan. (August 2016).
Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin.
,
(),
-
. Retrieved from
http://hdl.handle.net/10342/8449
MLA:
Chalovich, Joseph, and Johnson, Dylan.
"Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin". .
. (),
August 2016.
September 30, 2023.
http://hdl.handle.net/10342/8449.
Chicago:
Chalovich, Joseph and Johnson, Dylan,
"Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin," , no.
(August 2016),
http://hdl.handle.net/10342/8449 (accessed
September 30, 2023).
AMA:
Chalovich, Joseph, Johnson, Dylan.
Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin. .
August 2016;
():
.
http://hdl.handle.net/10342/8449. Accessed
September 30, 2023.
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