Sliding Filament Thory, with Ref to Upper Arm.

There are about 600 muscles in the body working together to create movement. Muscle contractions pull both ends of the muscle towards one another. One bone attached to each muscle is always more stabilized than the other. The less stabilized bone moves during muscle contraction due to the weaker stability. The points of attachment determine which bone will move. The least movable part is called the origin; it is the part that attaches closer to the midline of the body. This leaves the most movable part called the insertion. Each of these points can be identified in individual muscles to assist trainers in understanding how the muscles and joints work together to create motion.

The article Why Muscles Don’t Break: New Research Offers Possibilities for MD Therapies explains in-depth the functions of the muscles in the human body. Throughout the article the author, Joana Fernandes, presents the extensive amount of research that she has performed regarding this insightful topic. She cites a study published in the Proceedings of the National Academy of Sciences, called “α-Actinin/titin interaction: A Dynamic and Mechanically Stable Cluster of Bonds in the Muscle Z-disk”. Essentially, the study explains that the reason muscles don’t break is due to the two binding proteins called a-actinin and titin. Fernandes utilizes evidence from the study to formulate her article and describe how these two proteins work together in unison to withstand a force of up to five piconewtons, “The experiment showed the bond between these two proteins is able to withstand a force of five piconewtons, a small force comparable to nearly one billionth the weight of a bar of chocolate” (Fernandes). As the article progresses, Fernandes analyzes how such small forces hold a muscle together for a lifetime and explains to the reader that this is possible because there is seven times more strands of a-actinin than titin.

The sarcomeres are grouped into two types of filaments, actin filaments and myosin filaments. Actin filaments are thin protein fibers that are pulled to cause muscle contraction. The ends of the actin filaments

Those arrangements are the agonist, antagonist, and synergists which are responsible for the production of movements. Agonists muscle are also known as “prime movers or bicep brachii” they produce the main movement or sequences of movements via their own contractions in order to create a movement. Agonist muscles are usually organized in a way where they cross a joint through the tendon (Boundless, 2016). Antagonist muscles perform as opposing muscles to agonists. This means that they are responsible for returning the limb(s) to its original resting position. Synergist muscles are in control around a moveable joint to produce motion similar to the agonist muscles. They are responsible for the reduction of excessive force to create smooth muscle movements and they are also referred to as neutralizers (Boundless, 2016). Whenever, it is that the muscles contract they will pull on the bones in which they are attached in order to produce movement in the

The skeletal muscles connect to the bones and work with connective tissues at the joints to allow for movement.

Abstract- Within skeletal muscle, it contain a lot of myofibrils, within each myofibre are thousands of parallel myofibrils that are build-up of many sarcomeres (Sawatari 2016), the thick (myosin) and thin (actin) filaments in the sarcomere which play a play role on muscle concentration. When the myosin head crossbridge to actin filament, move the actin toward to the centre of sarcomere, and this process fueled by ATP and regulated by Ca2+ (Syd1.kuracloud.com 2016). The muscle was placed in a force transducer. Extracellular stimulating electrodes were attached near the pelvic end and recording electrodes near

The in vitro cell cultures were used first to determine the role in Myo1c in the start and ending for kinesin-1 transport on the actin filament and microtubule intersection. By tagging the kinesin-1 with fluorescences and placing the protein attached in environments with or without Myo1c, there could be an investigation on how the protein moves a synthesized cargo around the cell. From these results, it is noticed that Myo1c is helpful in the initiation of kinesin-1 runs on microtubules. The cargo docking at the AF intersections were shown to be specific to Myo1c. By using α-actinin to stop cargo at the same point as Myo1c, there was a distinct difference in the efficiency of pause in transport. This results of the α-actinin caused stops were shorter and less frequent than the Myo1c caused stops supporting the thought that these distinct stops are unique to Myo1c motor proteins. In order to test the effect non-muscle tropomyosins have on the Myo1c motor proteins experiments looking at the interaction between full length Tm2 and Myo1c, and how this interaction changes the AF/MT intersection were performed. Testing the Tm2-actin gliding inhibited how in the presence of Tm2, the Myo1c was prevented from pausing the cargo as it approached the Tm2-AF/MT

The sliding fiber hypothesis is a clarification of how muscle withdrawals happen. This hypothesis expresses that the actin fibers inside the sarcomere slide toward each other amid compression. Be that as it may, the myosin fibers don’t move. The second sort of muscle is smooth, which is found in inside organs and veins. It comprises of accumulations of fusiform cells that don’t demonstrate its striations under even a light magnifying instrument. The most well-known capacity of this muscle is to crush, which advances weight on the space inside the tube or organ it encompasses. Withdrawals of smooth muscle are feeble and moderate contrasted and the constrictions of the other two sorts. The smooth muscle withdrawals are and large controlled unknowingly by the autonomic sensory system, so in this manner the smooth muscle is a case of an automatic

2. Cartilaginous/slightly moveable joints exist at the ends of bone and are covered in hyaline

Muscle contains two type of important proteins which are myosin for thick filament and actin for the thin filament. The types of muscle can be categorized as skeletal muscle: attached directly or indirectly to the skeleton, smooth muscle: nonstriated appearance and no ordered myofibrils, and cardiac muscle: muscle of the hard with presence of intercalated disks. The process of myogenesis, forms tubular muscle cells which are myocytes (muscle fibers or myofibers) in skeletal muscle. Myofibers contain myofibrils, composed of repeating sections of sarcomeres.

The three myofilaments, the thick filaments, the thin filaments, and the elastic filaments, are the microfilaments that comprise the myofibril. The thick filament is made of many myosin molecules with a dual-globular head and a short, stubby tail. On the other hand, the thin filament is made of many inter-woven strands of fibrous actin with molecules of fibrous tropomyosin distributed along the thin filament. Each tropomyosin molecule has a troponin complex that can bind calcium ions, and upon calcium binding, it induces a conformational change within tropomyosin that exposes the myosin-binding sites on the actin filaments. Elastic filaments are made of titin that is attached to the Z disc weaves through the center of thick filament (Martini, Nath, and Bartholomew, 283-287).

Myosin can hydrolyze a single ATP in 30 seconds which is slow when compared to the 5-10 ATP hydrolyzed every second when combined with Actin[7]. One Myosin head binds to one Actin filament to hydrolyze ATP, this occurs due to the polarity of the Actin molecule[7][Img2]. After completion of the hydrolyzation process and release of the products the usually weak bond between Myosin and Actin is strengthened due to the release of Phosphate[6]. This change is referred to as the “Power Stroke”’ as it pulls the Actin filament down the line, ADP is released and the Myosin head detaches once a new ATP is secured so the process can repeat[1][Img2].

ATP will bind to myosin, being hydrolyzed by ATP and resulting into ADP and phosphate. This is where the energy come to support this process. The energy that comes from ATP being transformed into ADP and phosphate activates the myosin, leaving it in an extended position. The activated myosin will bind to an active

1. Ok so the sliding filament theory is basically the contraction of the sacromere. Calcium released from an ion channel bind to troponin which lies on the thick filament known as the actin. This then causes the tropomyosin to reveal on the actin. The myosin head then releases a phosphate from an ATP which causes then forms a cross bridge attaching both thick and thin filament. Causing one muscle contraction.

D. Both the shoulder and the hip are ball and socket joints. Why does the shoulder have a greater range of motion than the hip?