A mutation in troponin that increased itsaffinity for its ligand would lead to↑ # of myosin binding to actinI muscle contraction↑ muscle relaxation↑ [calcium] binding to calmodulin

Troponin protein helps to make muscle in rest Condition with the help of tropomyosin protein

Answered: A mutation in troponin that increased…

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A mutation in troponin that increased its affinity for its ligand would lead to

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter38: The Musculoskeletal System

Section: Chapter Questions

Problem 3VCQ: Figure 38.38 The deadly nerve gas Sarin irreversibly inhibits acetycholinesterase. What effect would...

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Concept explainers

Electron Transport Chain

The electron transport chain, also known as the electron transport system, is a group of proteins that transfer electrons through a membrane within mitochondria to create a gradient of protons that drives adenosine triphosphate (ATP)synthesis. The cell uses ATP as an energy source for metabolic processes and cellular functions. ETC involves series of reactions that convert redox energy from NADH (nicotinamide adenine dinucleotide (NAD) + hydrogen (H)) and FADH2(flavin adenine dinucleotide (FAD)) oxidation into proton-motive force(PMF), which is then used to synthesize ATP through conformational changes in the ATP synthase complex, a process known as oxidative phosphorylation.

Metabolism

Picture a campfire. It keeps the body warm on a cold night and provides light. To ensure that the fire keeps burning, fuel needs to be added(pieces of wood in this case). When a small piece is added, the fire burns bright for a bit and then dies down unless more wood is added. But, if too many pieces are placed at a time, the fire escalates and burns for a longer time, without actually burning away all the pieces that have been added. Many of them, especially the larger chunks or damp pieces, remain unburnt.

Cellular Respiration

Cellular respiration is the cellular process involved in the generation of adenosine triphosphate (ATP) molecules from the organic nutritional source obtained from the diet. It is a universal process observed in all types of life forms. The glucose (chemical formula C6H12O6) molecules are the preferred raw material for cell respiration as it possesses a simple structure and is highly efficient in nature.

Question

A mutation in troponin that increased its
affinity for its ligand would lead to
↑ # of myosin binding to actin
I muscle contraction
↑ muscle relaxation
↑ [calcium] binding to calmodulin

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ctions in smooth muscle cells depend on which one of the following activation steps? Ca2+-activated phosphorylation of myosin-II Ca²+ binding to troponin GTP binding to myosin-II Actin polymerization (b) (c) (d) Explain:
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…
What 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 actine
Protein-X has a calcium (Ca²+)-binding regulatory subunit. Upon calcium (Ca²+) binding the protein changes its own conformation resulting in the conformation change of protein-Y. As a result of this calcium (Ca²+)-dependent protein-X mediated conformational change protein-Y exposes the myosin II head binding sites on the skeletal muscle actin filaments. Identify the protein-X and protein-Y from the following choices. O Protein-X: Troponin; Protein-Y: Tropomysosin O Protein-X: Tropomodulin; CapZ O Protein-X: Nebulin; Protein-Y: Titin Protein-X: Tropomysosin; Protein-Y: Tropomodulin
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?
Arrange the following
Why is myosin II the only myosin capable of producing contractile force?
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.
During 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 fiber
1. a) Why are muscles not in a contracted state all the time? b) Several hours after the death of an animal, a state of rigor mortis, extreme rigidity of the body, occurs. With respect to myosin and actin filaments, why does this occur? What causes the body to relax more later in time? Explain.
What is the reaction catalyzed by the ATPase domain of myosin?
What happens to contraction of a muscle cell if some of the Ca2+ that was released during a contraction is still in the cytoplasm (sarcoplasm) when the next stimulus arrives? - The muscle contracts with the same tension generated as during the first contraction, because the number of cross-bridges formed is always the same during a contraction. - The muscle contracts with greater tension generated because more troponin molecules bound means greater myosin-binding sites (active sites) are revealed on the actin, leading to a larger number of cross-bridges formed. - The muscle contracts with greater tension generated because there will be more Ca2+ in the sarcoplasm after the second stimulation, which will bind to more troponin molecules. - The muscle contracts with the same tension generated as during the first contraction, because muscles contract in an all-or-none fashion.