Loose Leaf For Integrated Principles Of Zoology
18th Edition
ISBN: 9781260411140
Author: Cleveland P Hickman Jr. Emeritus, Susan L. Keen, David J Eisenhour Professor PhD, Allan Larson, Helen I'Anson Associate Professor of Biology
Publisher: McGraw-Hill Education
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Chapter 29, Problem 11RQ
Summary Introduction
To explain: The way how the actin and myosin proteins interact during the ameboid movement.
Introduction: A crucial characteristic of animals is movement. Animal movement takes place in various forms in animal tissues, for example, movements of skeletal muscles. However, most animal movements are based on a single fundamental mechanism such as contractile proteins.
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An unexpected discovery from studies of ameboid movement is that the same proteins found in the contractile system of animal muscle—actin and myosin—are present in ameboid cells. Explain how these and other proteins interact during ameboid movement.
Certain multi-headed myosins bind cooperatively to actin filaments. The binding interaction is mainly electrostatic in nature, so the presence of additional salt (ions) in solution can interfere with binding; ions will tend to associate with charged residues on the two proteins, blocking electrostatic attractions that would otherwise take place. Briefly describe the expected shape of the binding curve for one of these myosins, and what will happen to the shape when the salt concentration increases.
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…
Chapter 29 Solutions
Loose Leaf For Integrated Principles Of Zoology
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- The 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_forwardDescribe the movement of myosin along an actin filament. Outline the primary molecular steps and explain how this process is used by cells. How many actin monomers within an actin filament would a myosin molecule need to ratchet in order to contract a cell by approximately 1 um? How fast could a non-muscle cell make this contraction compared to a muscle cell if the relative rates of myosin walks on F-actin are 4.5 um/sec and 0.04 um/sec for myosin II and I respectively?arrow_forwardThe ability of myosin to walk along an actin filament may be observed with the aid of an appropriately equipped microscope. Describe how such assays are typically performed. Why is ATP required in these assays? How can such assays be used to determine the direction of myosin movement or the force produced by myosin?arrow_forward
- Contraction in both skeletal and smooth muscles requires theinflux of Ca2+ into the cytoplasm. Compare and contrast thelocations and functions of the molecules to which Ca2+ binds inskeletal and smooth muscles, and explain the steps that lead tocross-bridge cycling in each type of muscle.arrow_forwardDuring 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_forwardDiscuss the following statement: “The basal lam-ina of muscle fibers serves as a molecular bulletin board,in which adjoining cells can post messages that direct thedifferentiation and function of the underlying cells.”arrow_forward
- 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_forwardDuring the cross-bridge in muscle cells, myosin motors hydrolyzes ATP as a fuel to create a pulling force on actin fibers. Please describe1) the myosin motors undergo different steps of ATP hydrolysis2) the state of the ATP nucleotide affects the binding and position of the myosin motor with respect to the actin fiberarrow_forwardMyosin II has a duty ratio of 10 percent, and its step size is 8 nm. In contrast, myosin V has a much higher duty ratio (about 70 percent) and takes 36-nm steps as it walks down an actin filament. What differences between myosin II and myosin V account for their different properties?arrow_forward
- You know from experience that skeletal muscle tires quite quickly, especially if there is not enough oxygen. Interestingly, shellfish such as clams can maintain a month-long contraction in the muscle that keeps the shell closed. No oxygen gets in this situation. These muscles have a different version of myosin called paramyosin. Knowing what you know about the cellular mechanism of muscle contraction, propose a hypothesis to explain how paramyosin might work.arrow_forwardWhat is the main order histological structure of sarcomere? * Z line bind with actine without interaction with myosin Interaction of actine and myosin with Z line Interaction of myosin and actine with Z line Interaction of Z line with myosin and actinearrow_forwardA typical relaxed sarcomere is about 2.3 µm in length and contracts to about 2 µm in length. Within the sarcomere, the thin filaments are about 1 um long and the thick filaments are about 1.5 um long. (a) Describe the overlap of thick and thin filaments in the relaxed and contracted sarcomere. (b) An individual "step" by a myosin head in one cycle pulls the thin filament about 15 nm. How many steps must each actin fiber make in one contraction?arrow_forward
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