Muscle Tissue 1. How is muscle tissue categorized? Muscle tissue is categorized by its shape‚ the number of nuclei‚ and the mechanism of stimulation. 2. a. Click the Smooth Muscle Tissue. Identify each of the following: Nucleus----- Smooth Fiber Muscle------------------ b. Describe smooth muscle control (voluntary or involuntary). Involuntary c. Name some smooth muscle functions (click the “Tissue Locations” button). Smooth
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and its interactions with Cofilin in pathways leading to Synaptic Plasticity Abstract Cofilin is an actin depolymerization factor responsible for severance of actin filaments in dendritic spines. Cofilin is activated upon de-phosphorylation via slingshot phosphatase (SSH) and deactivated when phosphorylated by LIM-kinase (LIMK). Phosphorylation of Cofilin results in polymerization of F-actin therefore formation of dendritic spines which is associated with LTP. Peptide drugs S3 and p-S3 are known
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Since the actin filaments are attached to the Z lines‚ the sarcomere shortens from both sides when actin filaments slide along the myosin filaments. the myosin filament pulls the actin along its length and the cross bridges of the myosin filaments attach to the actin filaments and exert the force on them to move. This step is known as the sliding filament theory. The sarcomere shortens without
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even smaller structures called actin which is a thin‚ contractile protein filament‚ containing ’active’ or ’binding’ sites and myosin filaments which are a thick‚ contractile protein filament‚ with Myosin Heads. These filaments slide in and out between each other to form a muscle contractions‚ this is why it is known as the sliding filament theory. Firstly I am going to explain how the filaments slide. In a relaxed muscle the cross bridges are detached from the actin filaments. When you muscle contracts
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pts. A maximum of 20 pts may be added to your first exam 20 x (correct pts / total pts) Question 1 Actin and tubulin form self-assembling polymers. Where on the filaments do subunits exchange with free monomers? Subunit exchange with free monomers occurs at the end of filaments. In actin filaments‚ subunits can be freely exchanged at both ends of the filament (pointed and barbed ends) until the actin formation reaches a steady state. At this point‚ the subunits are added to the barbed end and lost
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exposing the myosin binding sites on actin. This is the latent period‚ the lag time between stimulation and contraction. Myosin heads or cross bridges attach to actin binding sites on thin filaments. The sliding filament theory of a muscle contraction begins. When myosin binds to actin it pulls toward the m-line this is the “power stroke”. Once myosin head if flexed‚ ATP binding site is exposed and ATP binds to the head. Every single myosin head that attaches to actin has to have ATP. Now the myosin
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An actin myofilament is actually composed of what three different molecules? * Troponin - When Calcium binds to troponin‚ it changes shape‚ which moves tropomyosin away. This uncovers the actin binding site‚ which allows myosin to bind to actin and begin contraction. * Tropomyosin - Covers the myosin binding sites on actin. * G-actin 11. Myosin molecules make contact with actin via what structure? Cross-bridges - The chemical bond myosin molecule forms with the actin molecule
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through elecroblotting‚ and finally detects the proteins. When the results after every step is completed‚ the membrane is analyzed based on where the bands are present in the gel. It has been told that actin and myosin is present in fish‚ making it tougher to chew in most cases. To test the theory of actin and myosin being present in fish making it tougher to chew was the purpose of this experiment. The proteins from Rainbow trout‚ Catfish‚ Pollock‚ Salmon‚ Tilapia‚ Mahi-mahi‚ Cod‚
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joint 2. Which of the following is NOT associated with the thin filaments in skeletal muscle: a. tropomyosin b. *titin c. actin d. troponin e. nebulin 3. What produces the symptoms of rigor mortis following death? a. the storage vesicles for ATP begin to break down at death‚ leading to
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of contraction with actin and myosin and z-lines on each side. Calcium binds to the troponin protein‚ located on the actin filament. This allows tropomyosin to move‚ exposing the myosin head binding sites on actin. When the myosin heads bind to actin‚ this is known as the cross bridge. ADP and Pi molecules are released‚ causing myosin to pull on actin. This movement is known as the power stroke. To stop the contraction‚ ATP binds to the myosin head‚ and myosin detaches from actin‚ stopping the contraction
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