Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 47.1, Problem 2R
Summary Introduction
To review:
The role played by troponin subunits to control the contraction of skeletal muscle.
Introduction:
The troponin molecule is bound to the actin filament. It has three subunits that bind to three different components, which help in controlling the muscular contraction. The calcium ions, released from the sarcoplasmic reticulum plays an important role in the contraction of the skeletal muscle.
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As mentioned in class, one additional major use of ATP in skeletal muscle (besides
powering the myosin heads) is the recycling of calcium ions back into the sarcoplasmic
reticulum after depolarization. The resting concentration of Ca++ in the muscle cell
cytoplasm is about 50-100 nM, and the spike concentration after depolarization is about
10-20 μΜ.
a) Consider a single sarcomere. What is the number of free calcium ions within the
sarcomere at rest? What is the number of free calcium ions after depolarization?
b) The major ion pump responsible for calcium ion recycling is SERCA (sarco/endoplasmic
reticulum calcium ATPase). SERCA uses one molecule of ATP to pump two calcium ions,
and the resting level can be restored in about 10-20 ms. How many molecules of ATP are
used in a single sarcomere for pumping calcium in a single "twitch"?
c) Assume that a single "twitch" is sufficient to drive one sarcomere from its fully extended
length (about 2.5 µm) to its fully contracted length (about 1…
Why is adenosine triphosphate (ATP) used for muscle contraction?
Why is myosin II the only myosin capable of producing contractile force?
Chapter 47 Solutions
Life: The Science of Biology
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- Pluripotent stem cells undergo a number of changes as they progress through developmental stages to become the terminally differentiated cell type known as a skeletal muscle myofiber. a) Describe the stages and key anatomic and functional changes that occur during differentiation of myofibers. b) Despite the fact that myofibers are terminally differentiated, muscle can regenerate itself following a trauma or injury. Describe how this can occur.arrow_forwardWhat are the mechanisms for muscle contraction vs. relaxation in regards to myosin/thick filaments/thin filament movement? Is it true that if tropomysin blocks myosin sites, contraction ends and muscle relaxes?arrow_forwardThe sliding-filament model of skeletal-muscle contraction assumes a sliding or slipping of interdigitating filaments of actin and myosin. Electron micrographs show that during contraction the actin and my-osin filaments remain of constant length while the distance between Z lines shortens. Explain how this happens in terms of the molecular structure of the muscle filaments. What is the role of regulatory pro-teins (troponin and tropomyosin) in contraction?arrow_forward
- During an experiment, the protein troponin from a skeletal muscle fiber was removed. This resulted in the permanent exposure of the actin binding site. Predict how cross-bridge cycling in this skeletal muscle fiber would be affected in the absence of troponin.arrow_forwardWhen the neurotransmitter acetylcholine (ACh) binds the acetylcholine receptor (a GPCR) on muscle cells, it causes them to contract. ZIGGY, a chemical analog of ACh, also binds to the same acetylcholine receptor on muscle cells, but instead causes the muscle cells to relax. For this reason, it is sometimes prescribed as a muscle relaxer. Explain in 3-4 sentences how ZIGGY could cause muscle relaxation. How can both ZIGGY and ACh bind the same GPCR? And then how can they have different effects on the cells, despite binding to the same receptor on the same cells?arrow_forwardSkeletal muscle cells undergo contractions based on a molecular mechanism involving: 1)the sliding of actin and myosin filaments past each other without any change in filament length 2) the shortening of actin filaments following direct interaction with myosin 3) dynamic instability of microtubules 4)nonearrow_forward
- What ion is necessary for movement of the troponintropomyosin complex? What is the role of thesarcoplasmic reticulum in this process?arrow_forwardWhat is Myesin?arrow_forwardHow do the different structures and properties of myosin II and myosin V reflect their different functions in cells?arrow_forward
- What is myosin light-chain phosphatase?arrow_forwardAn antibody has been isolated that binds to F-actin but not to G-actin. Whatstructural feature(s) of F-actin do you suppose the antibody binds (i.e., howis the antibody able to distinguish between these two forms of actin)?arrow_forwardYou are attempting to crystallize the head group of a myosin-like muscle protein from a newly discovered vertebrate organism. Assuming that the protein structure is similar to other vertebrate myosins, which enzymes should you use to remove the myosin-like head group from the rest of the myosin-like protein? A) both trypsin and myosinase B) both trypsin and papain C) papain D) trypsin E) myosinasearrow_forward
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