The main proteins involved in muscle contraction are actin, myosin, tropomyosin, and troponin. Actin forms thin filaments that interact with myosin heavy chain thick filaments through a sliding filament mechanism. Calcium ions released from the sarcoplasmic reticulum bind to troponin C, exposing actin binding sites and initiating muscle contraction. Muscle relaxation occurs when calcium ions are reabsorbed by the sarcoplasmic reticulum, causing troponin to cover the actin binding sites and inhibit the actin-myosin interaction. ATP hydrolysis provides the energy for myosin to pull on actin filaments through its power stroke, resulting in muscle shortening and force generation during each contraction
The document discusses the mechanism of muscle contraction, which involves the sliding of actin and myosin filaments past each other, shortening the sarcomere. Muscle contraction is triggered by acetylcholine releasing calcium ions from the sarcoplasmic reticulum. Calcium ions bind to troponin, exposing binding sites on actin for myosin to form cross-bridges. Myosin hydrolyzes ATP to generate power strokes that slide actin inward, contracting muscles. Muscles relax as acetylcholinesterase breaks down acetylcholine, calcium ions are pumped back into the sarcoplasmic reticulum, and cross-bridges detach.
The internal structure of skeletal muscle contains myofibrils made of thick and thin filaments that slide past each other. Thick filaments are composed of the protein myosin, while thin filaments are composed of actin. When calcium ions are released, they trigger the cross-bridge cycling of myosin binding and pulling on actin, causing muscle contraction. This sliding filament mechanism is how skeletal muscle generates force.
This document discusses muscular contraction and energy generation in mechanochemical systems. It explains that muscle contraction occurs via the sliding filament model, where thick and thin filaments containing the proteins actin and myosin slide past one another, shortening the muscle fibers. ATP hydrolysis by the myosin ATPase provides the energy for this process. Calcium ions play a key role in regulating contraction by initiating the interaction of actin and myosin. Phosphagens like creatine phosphate help replenish ATP levels and allow sustained muscle contraction.
The document summarizes the structure and function of skeletal muscle. Skeletal muscle is composed of bundles of muscle fibers which contain myofibrils made of actin and myosin filaments. The basic contractile unit is the sarcomere, where the overlapping actin and myosin filaments slide past each other to cause muscle contraction. Contraction is triggered by calcium ions released from the sarcoplasmic reticulum in response to an action potential, which allows myosin to bind to and pull on actin, shortening the muscle.
This document discusses the structure and function of skeletal muscle. It begins with an introduction to skeletal muscle and describes the characteristics of muscle fibers, including that they are multinucleated and striated. It then details the structure of the sarcomere, the basic contractile unit of skeletal muscle, including the thin actin filaments and thick myosin filaments. The document also describes excitation-contraction coupling and the sliding filament model of muscle contraction in which myosin cross-bridges attach to actin and generate force through an ATP-fueled cycling process.
Chemical and molecular basis of muscle contractionChirag Dhankhar
here in this ppt I have told about the different types of muscles their biological cycle of muscle contraction, needs of contraction, neural network working for muscle contraction, atp and cp energy use in muscles , how energy is used and made by muscles in middle of the exercise, anatomy of muscles, working of muscles, different types of bands and proteins needed for muscle contraction
Actin filaments, usually in association with myosin, are responsible for many types of cell movements. Myosin is the prototype of a molecular motor—a protein that converts chemical energy in the form of ATP to mechanical energy, thus generating force and movement. The most striking variety of such movement is muscle contraction, which has provided the model for understanding actin-myosin interactions and the motor activity of myosin molecules. However, interactions of actin and myosin are responsible not only for muscle contraction but also for a variety of movements of nonmuscle cells, including cell division, so these interactions play a central role in cell biology. Moreover, the actin cytoskeleton is responsible for the crawling movements of cells across a surface, which appear to be driven directly by actin polymerization as well as actin-myosin interactions.
The main proteins involved in muscle contraction are actin, myosin, tropomyosin, and troponin. Actin forms thin filaments that interact with myosin heavy chain thick filaments through a sliding filament mechanism. Calcium ions released from the sarcoplasmic reticulum bind to troponin C, exposing actin binding sites and initiating muscle contraction. Muscle relaxation occurs when calcium ions are reabsorbed by the sarcoplasmic reticulum, causing troponin to cover the actin binding sites and inhibit the actin-myosin interaction. ATP hydrolysis provides the energy for myosin to pull on actin filaments through its power stroke, resulting in muscle shortening and force generation during each contraction
The document discusses the mechanism of muscle contraction, which involves the sliding of actin and myosin filaments past each other, shortening the sarcomere. Muscle contraction is triggered by acetylcholine releasing calcium ions from the sarcoplasmic reticulum. Calcium ions bind to troponin, exposing binding sites on actin for myosin to form cross-bridges. Myosin hydrolyzes ATP to generate power strokes that slide actin inward, contracting muscles. Muscles relax as acetylcholinesterase breaks down acetylcholine, calcium ions are pumped back into the sarcoplasmic reticulum, and cross-bridges detach.
The internal structure of skeletal muscle contains myofibrils made of thick and thin filaments that slide past each other. Thick filaments are composed of the protein myosin, while thin filaments are composed of actin. When calcium ions are released, they trigger the cross-bridge cycling of myosin binding and pulling on actin, causing muscle contraction. This sliding filament mechanism is how skeletal muscle generates force.
This document discusses muscular contraction and energy generation in mechanochemical systems. It explains that muscle contraction occurs via the sliding filament model, where thick and thin filaments containing the proteins actin and myosin slide past one another, shortening the muscle fibers. ATP hydrolysis by the myosin ATPase provides the energy for this process. Calcium ions play a key role in regulating contraction by initiating the interaction of actin and myosin. Phosphagens like creatine phosphate help replenish ATP levels and allow sustained muscle contraction.
The document summarizes the structure and function of skeletal muscle. Skeletal muscle is composed of bundles of muscle fibers which contain myofibrils made of actin and myosin filaments. The basic contractile unit is the sarcomere, where the overlapping actin and myosin filaments slide past each other to cause muscle contraction. Contraction is triggered by calcium ions released from the sarcoplasmic reticulum in response to an action potential, which allows myosin to bind to and pull on actin, shortening the muscle.
This document discusses the structure and function of skeletal muscle. It begins with an introduction to skeletal muscle and describes the characteristics of muscle fibers, including that they are multinucleated and striated. It then details the structure of the sarcomere, the basic contractile unit of skeletal muscle, including the thin actin filaments and thick myosin filaments. The document also describes excitation-contraction coupling and the sliding filament model of muscle contraction in which myosin cross-bridges attach to actin and generate force through an ATP-fueled cycling process.
Chemical and molecular basis of muscle contractionChirag Dhankhar
here in this ppt I have told about the different types of muscles their biological cycle of muscle contraction, needs of contraction, neural network working for muscle contraction, atp and cp energy use in muscles , how energy is used and made by muscles in middle of the exercise, anatomy of muscles, working of muscles, different types of bands and proteins needed for muscle contraction
Actin filaments, usually in association with myosin, are responsible for many types of cell movements. Myosin is the prototype of a molecular motor—a protein that converts chemical energy in the form of ATP to mechanical energy, thus generating force and movement. The most striking variety of such movement is muscle contraction, which has provided the model for understanding actin-myosin interactions and the motor activity of myosin molecules. However, interactions of actin and myosin are responsible not only for muscle contraction but also for a variety of movements of nonmuscle cells, including cell division, so these interactions play a central role in cell biology. Moreover, the actin cytoskeleton is responsible for the crawling movements of cells across a surface, which appear to be driven directly by actin polymerization as well as actin-myosin interactions.
This document summarizes the mechanism of muscle contraction. It discusses:
- Motor units consisting of motor neurons and muscle fibers.
- The sliding filament theory proposed by Huxley and Hanson which explains contraction in three steps: depolarization, contraction, and relaxation.
- During depolarization, acetylcholine is released causing calcium release and muscle fiber depolarization.
- Contraction occurs as calcium binds troponin, exposing actin binding sites and allowing cross-bridge cycling to occur as myosin heads pull actin fibers.
- Relaxation happens as calcium is reabsorbed, troponin moves back, and cross-bridges detach, relaxing the muscle.
Muscles contract through a sliding filament mechanism where actin and myosin filaments interact. Energy from ATP hydrolysis causes the myosin head to undergo conformational changes, attaching and detaching from actin and sliding the filaments past each other. This shortens the sarcomere. Tropomyosin normally blocks the actin binding sites, but calcium released during muscle stimulation displaces tropomyosin, allowing the cross-bridge cycle and contraction. When calcium is reabsorbed, tropomyosin resets and the muscle relaxes.
This document summarizes the mechanism and chemical changes that occur during muscle contraction. It describes the structure of the sarcomere including the myofibrils, bands, and essential contractile proteins actin and myosin. The sliding filament mechanism is explained whereby calcium release allows the myosin heads to bind to actin and pull the thin filaments inward through a power stroke, shortening the sarcomere and causing muscle contraction. Key chemical events include the utilization of ATP to polymerize G-actin to F-actin and for the binding of actomyosin, with ATP hydrolysis providing energy for the power stroke. ATP is then rephosphorylated through phosphagen and carbohydrate breakdown pathways to allow for repeated contractions.
Skeletal muscle is composed of bundles of muscle fibers wrapped in connective tissue sheaths. Each muscle fiber contains myofibrils which are made of repeating contractile units called sarcomeres. Sarcomeres contain thick myosin filaments interdigitating with thin actin filaments. During muscle contraction, cross bridges extending from the myosin filaments attach to the actin filaments, causing the sarcomere to shorten and the muscle fiber to contract.
1. The document describes the structure and function of striated muscle, including the microscopic structure of myofibrils and sarcomeres.
2. It explains the sliding filament theory of muscle contraction, where an action potential triggers the release of calcium ions which allow myosin to bind to actin, forming cross-bridges that pull the filaments together through a power stroke, shortening the muscle.
3. The contraction cycle involves myosin binding to actin binding sites after ATP splits, bending myosin and shortening the sarcomere, before detaching when new ATP binds.
- Skeletal muscle makes up 40% of total body mass and contains long, striated muscle fibers that are multinucleated.
- Each muscle fiber contains numerous myofibrils composed of thin actin filaments and thick myosin filaments that overlap to form dark A bands and light I bands.
- The functional unit of skeletal muscle is the sarcomere, defined as the segment between two Z disks, which contains overlapping actin and myosin filaments that slide past each other during muscle contraction.
- Excitation-contraction coupling involves an action potential triggering calcium release from the sarcoplasmic reticulum, allowing calcium to bind troponin and initiate the contraction of actin and myosin
2nd and 3rd September 2011,a General Lecture Theatre, Dr Chirantan Mandal, Dr Avik Basu, Dr Dipayan Sen Dr Ushnish Adhikari,Dr Srimanti Bhattacharya, Dr Shubham Presided by Dr Arnab Sengupta (Physiology Dept Medical College Kolkata)
1. The document discusses the mechanism of muscle contraction known as excitation-contraction coupling, where an action potential causes the myofibrils in muscle to contract.
2. It describes the structures involved in muscle contraction including myofibrils, sarcoplasmic reticulum, transverse tubules, thick and thin filaments, and sarcomeres.
3. The mechanism of muscle contraction involves calcium release from the sarcoplasmic reticulum in response to an action potential, which allows cross-bridge binding of actin and myosin filaments and the sliding filament mechanism of contraction.
The document summarizes the structure and function of skeletal muscle myosin and actin filaments during muscle contraction. It describes how myosin filaments are composed of myosin molecules that form cross-bridges with heads that can interact with actin filaments. Actin filaments contain actin, tropomyosin and troponin. Calcium released from the sarcoplasmic reticulum activates contraction by allowing the myosin heads to bind to active sites on actin. The myosin heads then tilt and pull the actin filaments towards the center in a ratcheting motion, powered by ATP hydrolysis.
Muscle contraction occurs via the sliding filament mechanism. The myosin heads attach to actin and pull the filaments together, shortening the sarcomere. Calcium ions trigger muscle contraction by binding to troponin and exposing myosin binding sites on actin. Myosin then hydrolyzes ATP to generate the force needed for cross-bridge cycling and filament sliding. Relaxation occurs when calcium is pumped back into the sarcoplasmic reticulum, removing it from the myofilaments. Motor units, each innervated by a motor neuron, allow graded muscle responses through recruitment of additional fibers.
(1) Muscle converts chemical energy from ATP into mechanical force via contraction. There are three main muscle types: skeletal, cardiac, and smooth.
(2) Skeletal muscle fibers contain thick myosin filaments that interact with thin actin filaments to generate force. Calcium binds to troponin, allowing this interaction and contraction.
(3) Cardiac muscle relies more on extracellular calcium for contraction due to less extensive calcium stores. Calcium enters through membrane channels and is released from sarcoplasmic reticulum stores via calcium-induced calcium release.
Muscle cells contain myofibrils which are composed of actin, myosin, and titin proteins organized into thin filaments, thick filaments, and sarcomeres. Actin exists as globular G-actin monomers or polymerized F-actin in microfilaments and thin filaments. Myosin is a motor protein with a head, neck, and tail domain that binds actin and uses ATP hydrolysis. Muscle contraction occurs when actin thin filaments slide over myosin thick filaments, known as the sliding filament theory, in a calcium-dependent process where the power stroke of myosin pulls actin toward the center of the sarcomere.
The document describes the structure and function of myofilaments in muscle cells. It discusses that myosin forms thick filaments with heads that project from the filament and act as cross bridges. Actin forms thin filaments along with the proteins tropomyosin and troponin. Contraction occurs when cross bridges attach to actin filaments and cause them to slide inward towards the center of the sarcomere, shortening the muscle cell. Calcium released during muscle stimulation allows cross bridge attachment and the hydrolysis of ATP provides energy for the cross bridges to pull on actin, resulting in contraction.
This document summarizes the major proteins involved in muscle structure and contraction. It discusses the roles of actin, tropomyosin, and troponin in forming the thin filaments, and how actin polymerizes. Myosin forms the thick filaments and interacts with actin to generate force through ATP hydrolysis. The contraction cycle involves the actin-myosin complex forming and breaking through ATP binding and hydrolysis. Muscle derives ATP from glycolysis, oxidative phosphorylation, and creatine phosphate to power continuous contractions. Genetic mutations can cause muscular dystrophy where muscles progressively deteriorate.
The document describes various aspects of muscle contraction including:
1) Excitation-contraction coupling which involves depolarization of the muscle membrane leading to calcium release and muscle contraction.
2) The roles of the sarcoplasmic reticulum, t-tubules, and troponin-tropomyosin complex in regulating calcium levels and exposing actin binding sites during contraction.
3) The sliding filament theory of how myosin heads binding to actin causes muscle shortening through an ATP-driven cycling of cross-bridge formation and breaking.
1. The document discusses the structure and function of the neuromuscular junction and skeletal muscle contraction. It describes how an action potential causes the release of acetylcholine from the motor neuron, leading to depolarization of the muscle fiber membrane.
2. Calcium release within the muscle fiber initiates cross-bridge cycling between actin and myosin, producing muscle contraction. Contraction ceases as calcium is reabsorbed by the sarcoplasmic reticulum, relaxing the muscle.
3. The length-tension relationship states that skeletal muscle generates maximum force when sarcomeres are at their optimal resting length, with overlapping actin and myosin filaments. Shorter or longer lengths reduce the number of cross-
Actin and myosin are proteins that play important roles in muscle contraction. Actin exists as monomers called G-actin and polymers called F-actin that form microfilaments. Myosin has a head domain that binds to actin and uses ATP to generate force and move along actin filaments. During muscle contraction, myosin heads attach to actin, exert tension through a power stroke, causing actin filaments to slide and muscles to shorten. Precise interactions between actin and myosin are crucial for muscle function and movement.
1. The document discusses the structure and function of skeletal muscle tissue. It describes the microscopic anatomy of skeletal muscle fibers and their myofibrils, sarcomeres, and filaments.
2. The contraction process is summarized, from the generation of an action potential to the sliding filament model. Key steps include calcium release, troponin/tropomyosin interaction, cross-bridge cycling powered by ATP hydrolysis.
3. Different types of muscle contractions - isometric, isotonic - and motor unit activation patterns - twitch, tetanus - are defined. Stimulus intensity controls muscle force through graded motor unit recruitment.
The muscle are biological motors which convert chemical energy into force and mechanical work.
This biological machinery is composed of proteins – which is actomyosin and the fuel is ATP.
With the use of muscles we are able to act on our environment.
Muscle movement plays an important role in day to day life where the contraction and relaxation of muscle is significant. The current slide has been developed with the focus on different phases during muscle contraction and the physiological change involved on it.
1. The sliding filament theory of muscle contraction describes how myosin cross-bridges interact with actin filaments through ATP hydrolysis, generating force and causing filament sliding.
2. Calcium binding to troponin exposes actin binding sites, allowing myosin cross-bridge binding and force generation through its power stroke.
3. Repeated myosin cross-bridge cycling causes incremental filament sliding, shortening the sarcomere and generating muscle contraction. ATP is required to detach cross-bridges between cycles.
This document summarizes the mechanism of muscle contraction. It discusses:
- Motor units consisting of motor neurons and muscle fibers.
- The sliding filament theory proposed by Huxley and Hanson which explains contraction in three steps: depolarization, contraction, and relaxation.
- During depolarization, acetylcholine is released causing calcium release and muscle fiber depolarization.
- Contraction occurs as calcium binds troponin, exposing actin binding sites and allowing cross-bridge cycling to occur as myosin heads pull actin fibers.
- Relaxation happens as calcium is reabsorbed, troponin moves back, and cross-bridges detach, relaxing the muscle.
Muscles contract through a sliding filament mechanism where actin and myosin filaments interact. Energy from ATP hydrolysis causes the myosin head to undergo conformational changes, attaching and detaching from actin and sliding the filaments past each other. This shortens the sarcomere. Tropomyosin normally blocks the actin binding sites, but calcium released during muscle stimulation displaces tropomyosin, allowing the cross-bridge cycle and contraction. When calcium is reabsorbed, tropomyosin resets and the muscle relaxes.
This document summarizes the mechanism and chemical changes that occur during muscle contraction. It describes the structure of the sarcomere including the myofibrils, bands, and essential contractile proteins actin and myosin. The sliding filament mechanism is explained whereby calcium release allows the myosin heads to bind to actin and pull the thin filaments inward through a power stroke, shortening the sarcomere and causing muscle contraction. Key chemical events include the utilization of ATP to polymerize G-actin to F-actin and for the binding of actomyosin, with ATP hydrolysis providing energy for the power stroke. ATP is then rephosphorylated through phosphagen and carbohydrate breakdown pathways to allow for repeated contractions.
Skeletal muscle is composed of bundles of muscle fibers wrapped in connective tissue sheaths. Each muscle fiber contains myofibrils which are made of repeating contractile units called sarcomeres. Sarcomeres contain thick myosin filaments interdigitating with thin actin filaments. During muscle contraction, cross bridges extending from the myosin filaments attach to the actin filaments, causing the sarcomere to shorten and the muscle fiber to contract.
1. The document describes the structure and function of striated muscle, including the microscopic structure of myofibrils and sarcomeres.
2. It explains the sliding filament theory of muscle contraction, where an action potential triggers the release of calcium ions which allow myosin to bind to actin, forming cross-bridges that pull the filaments together through a power stroke, shortening the muscle.
3. The contraction cycle involves myosin binding to actin binding sites after ATP splits, bending myosin and shortening the sarcomere, before detaching when new ATP binds.
- Skeletal muscle makes up 40% of total body mass and contains long, striated muscle fibers that are multinucleated.
- Each muscle fiber contains numerous myofibrils composed of thin actin filaments and thick myosin filaments that overlap to form dark A bands and light I bands.
- The functional unit of skeletal muscle is the sarcomere, defined as the segment between two Z disks, which contains overlapping actin and myosin filaments that slide past each other during muscle contraction.
- Excitation-contraction coupling involves an action potential triggering calcium release from the sarcoplasmic reticulum, allowing calcium to bind troponin and initiate the contraction of actin and myosin
2nd and 3rd September 2011,a General Lecture Theatre, Dr Chirantan Mandal, Dr Avik Basu, Dr Dipayan Sen Dr Ushnish Adhikari,Dr Srimanti Bhattacharya, Dr Shubham Presided by Dr Arnab Sengupta (Physiology Dept Medical College Kolkata)
1. The document discusses the mechanism of muscle contraction known as excitation-contraction coupling, where an action potential causes the myofibrils in muscle to contract.
2. It describes the structures involved in muscle contraction including myofibrils, sarcoplasmic reticulum, transverse tubules, thick and thin filaments, and sarcomeres.
3. The mechanism of muscle contraction involves calcium release from the sarcoplasmic reticulum in response to an action potential, which allows cross-bridge binding of actin and myosin filaments and the sliding filament mechanism of contraction.
The document summarizes the structure and function of skeletal muscle myosin and actin filaments during muscle contraction. It describes how myosin filaments are composed of myosin molecules that form cross-bridges with heads that can interact with actin filaments. Actin filaments contain actin, tropomyosin and troponin. Calcium released from the sarcoplasmic reticulum activates contraction by allowing the myosin heads to bind to active sites on actin. The myosin heads then tilt and pull the actin filaments towards the center in a ratcheting motion, powered by ATP hydrolysis.
Muscle contraction occurs via the sliding filament mechanism. The myosin heads attach to actin and pull the filaments together, shortening the sarcomere. Calcium ions trigger muscle contraction by binding to troponin and exposing myosin binding sites on actin. Myosin then hydrolyzes ATP to generate the force needed for cross-bridge cycling and filament sliding. Relaxation occurs when calcium is pumped back into the sarcoplasmic reticulum, removing it from the myofilaments. Motor units, each innervated by a motor neuron, allow graded muscle responses through recruitment of additional fibers.
(1) Muscle converts chemical energy from ATP into mechanical force via contraction. There are three main muscle types: skeletal, cardiac, and smooth.
(2) Skeletal muscle fibers contain thick myosin filaments that interact with thin actin filaments to generate force. Calcium binds to troponin, allowing this interaction and contraction.
(3) Cardiac muscle relies more on extracellular calcium for contraction due to less extensive calcium stores. Calcium enters through membrane channels and is released from sarcoplasmic reticulum stores via calcium-induced calcium release.
Muscle cells contain myofibrils which are composed of actin, myosin, and titin proteins organized into thin filaments, thick filaments, and sarcomeres. Actin exists as globular G-actin monomers or polymerized F-actin in microfilaments and thin filaments. Myosin is a motor protein with a head, neck, and tail domain that binds actin and uses ATP hydrolysis. Muscle contraction occurs when actin thin filaments slide over myosin thick filaments, known as the sliding filament theory, in a calcium-dependent process where the power stroke of myosin pulls actin toward the center of the sarcomere.
The document describes the structure and function of myofilaments in muscle cells. It discusses that myosin forms thick filaments with heads that project from the filament and act as cross bridges. Actin forms thin filaments along with the proteins tropomyosin and troponin. Contraction occurs when cross bridges attach to actin filaments and cause them to slide inward towards the center of the sarcomere, shortening the muscle cell. Calcium released during muscle stimulation allows cross bridge attachment and the hydrolysis of ATP provides energy for the cross bridges to pull on actin, resulting in contraction.
This document summarizes the major proteins involved in muscle structure and contraction. It discusses the roles of actin, tropomyosin, and troponin in forming the thin filaments, and how actin polymerizes. Myosin forms the thick filaments and interacts with actin to generate force through ATP hydrolysis. The contraction cycle involves the actin-myosin complex forming and breaking through ATP binding and hydrolysis. Muscle derives ATP from glycolysis, oxidative phosphorylation, and creatine phosphate to power continuous contractions. Genetic mutations can cause muscular dystrophy where muscles progressively deteriorate.
The document describes various aspects of muscle contraction including:
1) Excitation-contraction coupling which involves depolarization of the muscle membrane leading to calcium release and muscle contraction.
2) The roles of the sarcoplasmic reticulum, t-tubules, and troponin-tropomyosin complex in regulating calcium levels and exposing actin binding sites during contraction.
3) The sliding filament theory of how myosin heads binding to actin causes muscle shortening through an ATP-driven cycling of cross-bridge formation and breaking.
1. The document discusses the structure and function of the neuromuscular junction and skeletal muscle contraction. It describes how an action potential causes the release of acetylcholine from the motor neuron, leading to depolarization of the muscle fiber membrane.
2. Calcium release within the muscle fiber initiates cross-bridge cycling between actin and myosin, producing muscle contraction. Contraction ceases as calcium is reabsorbed by the sarcoplasmic reticulum, relaxing the muscle.
3. The length-tension relationship states that skeletal muscle generates maximum force when sarcomeres are at their optimal resting length, with overlapping actin and myosin filaments. Shorter or longer lengths reduce the number of cross-
Actin and myosin are proteins that play important roles in muscle contraction. Actin exists as monomers called G-actin and polymers called F-actin that form microfilaments. Myosin has a head domain that binds to actin and uses ATP to generate force and move along actin filaments. During muscle contraction, myosin heads attach to actin, exert tension through a power stroke, causing actin filaments to slide and muscles to shorten. Precise interactions between actin and myosin are crucial for muscle function and movement.
1. The document discusses the structure and function of skeletal muscle tissue. It describes the microscopic anatomy of skeletal muscle fibers and their myofibrils, sarcomeres, and filaments.
2. The contraction process is summarized, from the generation of an action potential to the sliding filament model. Key steps include calcium release, troponin/tropomyosin interaction, cross-bridge cycling powered by ATP hydrolysis.
3. Different types of muscle contractions - isometric, isotonic - and motor unit activation patterns - twitch, tetanus - are defined. Stimulus intensity controls muscle force through graded motor unit recruitment.
The muscle are biological motors which convert chemical energy into force and mechanical work.
This biological machinery is composed of proteins – which is actomyosin and the fuel is ATP.
With the use of muscles we are able to act on our environment.
Muscle movement plays an important role in day to day life where the contraction and relaxation of muscle is significant. The current slide has been developed with the focus on different phases during muscle contraction and the physiological change involved on it.
1. The sliding filament theory of muscle contraction describes how myosin cross-bridges interact with actin filaments through ATP hydrolysis, generating force and causing filament sliding.
2. Calcium binding to troponin exposes actin binding sites, allowing myosin cross-bridge binding and force generation through its power stroke.
3. Repeated myosin cross-bridge cycling causes incremental filament sliding, shortening the sarcomere and generating muscle contraction. ATP is required to detach cross-bridges between cycles.
Skeletal muscle is composed of long cylindrical muscle fibers that contain contractile filaments called myofibrils. Myofibrils contain regularly arranged thick and thin filaments that allow for muscle contraction via the sliding filament mechanism. Thick filaments are composed of myosin and thin filaments are composed of actin. When calcium levels rise, myosin heads bind to actin and the power stroke causes thin filaments to slide inward, shortening the sarcomere and muscle fiber. Calcium is released from the sarcoplasmic reticulum via T-tubules in response to neural stimulation.
Organisation of sarcomere.pdfehdshtdhserthSriRam071
The document discusses the structure and organization of muscle tissue. It describes the basic unit of muscle contraction, the sarcomere, which is composed of thin actin filaments and thick myosin filaments. It explains that sarcomeres are arranged in repeating patterns within myofibrils to give skeletal and cardiac muscles their striated appearance. Contraction occurs when myosin heads bind to actin and the filaments slide past each other. The sarcomere is regulated by troponin and tropomyosin on the actin filaments. The sarcoplasmic reticulum stores and releases calcium ions to control contraction.
EDITED- PART II- LOCOMOTION AND MOVEMENT – STRUCTURE,.pptxJagdeeshShetty2
The document summarizes the structure and function of muscle tissue. It describes the organization of proteins actin and myosin into thin and thick filaments within myofibrils. The sliding filament theory of muscle contraction is explained, where myosin heads bind to actin and use ATP to "walk" along the filaments, causing them to slide past each other and shorten the muscle. Two types of muscle fibers are also described: red fibers with many mitochondria and myoglobin that allow aerobic respiration and white fibers with fewer mitochondria that rely more on anaerobic glycolysis.
This document summarizes key aspects of muscle physiology:
1. It describes the three main types of muscle tissue - skeletal, cardiac, and smooth muscle - and their characteristic features such as number of nuclei and speed of contraction.
2. The structure and sliding filament mechanism of skeletal muscle contraction is explained. Key contractile proteins actin, myosin, and tropomyosin play a role in muscle shortening.
3. The process of excitation-contraction coupling is summarized, where an action potential triggers calcium release and cross-bridge cycling to cause muscle fiber contraction.
The document summarizes skeletal muscle contraction and excitation. It discusses the physiological anatomy of skeletal muscle fibers and their components. It then describes the general mechanism of muscle contraction initiated by a nerve impulse and action potential. On a molecular level, it explains the sliding filament theory and interactions between actin, myosin, calcium ions and ATP that cause contraction. Finally, it discusses the neuromuscular junction where motor neurons signal the muscle fiber and release acetylcholine to trigger muscle excitation.
This document summarizes the process of muscle excitation and contraction. It discusses how an action potential triggers the release of calcium ions, which then bind to troponin and allow the myosin heads to interact with actin filaments. The myosin heads undergo an ATP-powered power stroke that causes the filaments to slide past each other, resulting in muscle shortening and contraction. Muscle relaxation occurs when calcium ions are pumped back into the sarcoplasmic reticulum, detaching the myosin heads from actin and allowing the muscle fibers to return to their resting state.
This document discusses exercise physiology and the structure and function of exercising muscle. It begins by defining anatomy, physiology, exercise physiology, and sports physiology. It then describes the structure of muscle including the epimysium, perimysium, endomysium, plasmalemma, sarcoplasm, transverse tubules, and sarcoplasmic reticulum. It explains the sliding filament theory of muscle contraction which is driven by the hydrolysis of ATP and the release and reuptake of calcium. It concludes by describing the roles of the neuromuscular junction, action potentials, and calcium in initiating and ending muscle contraction.
This document provides an overview of muscle physiology, including:
1. The objectives are to learn about muscle functions, types, structures, contraction mechanisms, and differences between muscle fiber types.
2. Muscles have general functions like body movement, stabilization, substance transport, heat generation, and respiration.
3. Muscles are classified by control (voluntary or involuntary), location, and striation. The three main types are skeletal, cardiac, and smooth muscle.
4. Skeletal muscle contraction occurs via the sliding filament theory where the cross-bridge cycling of actin and myosin fibers causes sarcomere shortening and muscle contraction.
1) Skeletal muscle tissue is composed of long, cylindrical, multinucleated cells called muscle fibers that contract voluntarily to facilitate movement.
2) Muscle fibers are bundled together and surrounded by connective tissue layers including the endomysium, perimysium, and epimysium.
3) Contraction occurs via the sliding filament model, where the binding of calcium ions exposes actin binding sites on thin filaments, allowing myosin heads to interact and pull actin filaments inward, shortening the sarcomere and muscle fiber.
Muscle physiology in orthodontics/certified fixed orthodontic courses by Ind...Indian dental academy
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Molecular mechanism of Skeletal muscle contraction.2022.pptxTaroTari
The document summarizes the molecular mechanism of skeletal muscle contraction. It describes how skeletal muscle contraction occurs via a sliding filament mechanism where actin and myosin filaments interact. When calcium levels rise, myosin cross-bridges can bind to actin, and the power stroke of myosin causes the filaments to slide past each other, shortening the sarcomere and generating force. ATP provides the energy for myosin to detach from actin and re-attach, driving the cross-bridge cycle and continuous muscle contraction.
Anatomy of the masticatory machine. It consists of a fixed and a movable member. The movable member is activated by a series of voluntary muscles, and its efficiency is increased by another set of voluntary muscles that feed the machine.
Muscle fibers are single cylindrical cells composed of bundles of myofibrils, which contain actin and myosin filaments. There are three main types of muscle tissue - skeletal, cardiac, and smooth muscle. Skeletal muscle is striated, under voluntary control, and has multiple peripheral nuclei. The functional unit of skeletal muscle is the sarcomere, containing actin, myosin, and regulatory proteins. Contraction occurs via the sliding filament model, in which calcium binding allows myosin to interact with and pull actin filaments toward the center of the sarcomere.
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The document summarizes the structure and function of the muscular system. It discusses three main points:
1. There are three types of muscles, with skeletal muscles producing movement by pulling tendons. Skeletal muscles are composed of fascicles surrounded by connective tissue sheaths.
2. Skeletal muscle fibers contain myofibrils made up of repeating sarcomere units containing actin and myosin filaments. Contraction occurs via the sliding filament model as cross-bridges form between actin and myosin.
3. Calcium released from the sarcoplasmic reticulum binds to troponin, exposing actin binding sites and initiating the contraction cycle of cross-bridge formation and actin filament
This document discusses the structure and function of skeletal muscle. It describes the classification of muscles, the structure of muscle fibers including myofibrils and sarcomeres, and the molecular components actin and myosin that enable contraction. It explains that calcium triggers the interaction of actin and myosin heads, leading to muscle shortening. Energy for contraction comes initially from ATP and phosphocreatine, then from glycogen and oxidative metabolism. The document also distinguishes between isotonic contraction, where muscle length changes, and isometric contraction, where tension but not length changes.
Locomotion is the voluntary movement of organisms that results in a change of position. It occurs through locomotory movements like walking, running, climbing, flying, and swimming. Muscles enable locomotion and have properties like excitability, contractility, extensibility, and elasticity. There are three main types of muscles - skeletal muscles which are striated and attached to bones, visceral muscles which are smooth and located in organs, and cardiac muscles which make up the heart. Skeletal muscles enable locomotion through contraction initiated by motor neurons in the nervous system.
Molecular basis of Skeletal Muscle ContractionArulSood2
The ppt aims to explain the molecular basis of skeletal muscle contraction and certain applied aspects of the same. Sources include Guyton and Hall's Textbook of Physiology (South-Asia edition, Vol. 2) and C.L. Ghai's Textbook for Practical Physiology.
Travis Hills' Endeavors in Minnesota: Fostering Environmental and Economic Pr...Travis Hills MN
Travis Hills of Minnesota developed a method to convert waste into high-value dry fertilizer, significantly enriching soil quality. By providing farmers with a valuable resource derived from waste, Travis Hills helps enhance farm profitability while promoting environmental stewardship. Travis Hills' sustainable practices lead to cost savings and increased revenue for farmers by improving resource efficiency and reducing waste.
The debris of the ‘last major merger’ is dynamically youngSérgio Sacani
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
What is greenhouse gasses and how many gasses are there to affect the Earth.moosaasad1975
What are greenhouse gasses how they affect the earth and its environment what is the future of the environment and earth how the weather and the climate effects.
Phenomics assisted breeding in crop improvementIshaGoswami9
As the population is increasing and will reach about 9 billion upto 2050. Also due to climate change, it is difficult to meet the food requirement of such a large population. Facing the challenges presented by resource shortages, climate
change, and increasing global population, crop yield and quality need to be improved in a sustainable way over the coming decades. Genetic improvement by breeding is the best way to increase crop productivity. With the rapid progression of functional
genomics, an increasing number of crop genomes have been sequenced and dozens of genes influencing key agronomic traits have been identified. However, current genome sequence information has not been adequately exploited for understanding
the complex characteristics of multiple gene, owing to a lack of crop phenotypic data. Efficient, automatic, and accurate technologies and platforms that can capture phenotypic data that can
be linked to genomics information for crop improvement at all growth stages have become as important as genotyping. Thus,
high-throughput phenotyping has become the major bottleneck restricting crop breeding. Plant phenomics has been defined as the high-throughput, accurate acquisition and analysis of multi-dimensional phenotypes
during crop growing stages at the organism level, including the cell, tissue, organ, individual plant, plot, and field levels. With the rapid development of novel sensors, imaging technology,
and analysis methods, numerous infrastructure platforms have been developed for phenotyping.
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...University of Maribor
Slides from talk:
Aleš Zamuda: Remote Sensing and Computational, Evolutionary, Supercomputing, and Intelligent Systems.
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Inter-Society Networking Panel GRSS/MTT-S/CIS Panel Session: Promoting Connection and Cooperation
https://www.etran.rs/2024/en/home-english/
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...Sérgio Sacani
Context. With a mass exceeding several 104 M⊙ and a rich and dense population of massive stars, supermassive young star clusters
represent the most massive star-forming environment that is dominated by the feedback from massive stars and gravitational interactions
among stars.
Aims. In this paper we present the Extended Westerlund 1 and 2 Open Clusters Survey (EWOCS) project, which aims to investigate
the influence of the starburst environment on the formation of stars and planets, and on the evolution of both low and high mass stars.
The primary targets of this project are Westerlund 1 and 2, the closest supermassive star clusters to the Sun.
Methods. The project is based primarily on recent observations conducted with the Chandra and JWST observatories. Specifically,
the Chandra survey of Westerlund 1 consists of 36 new ACIS-I observations, nearly co-pointed, for a total exposure time of 1 Msec.
Additionally, we included 8 archival Chandra/ACIS-S observations. This paper presents the resulting catalog of X-ray sources within
and around Westerlund 1. Sources were detected by combining various existing methods, and photon extraction and source validation
were carried out using the ACIS-Extract software.
Results. The EWOCS X-ray catalog comprises 5963 validated sources out of the 9420 initially provided to ACIS-Extract, reaching a
photon flux threshold of approximately 2 × 10−8 photons cm−2
s
−1
. The X-ray sources exhibit a highly concentrated spatial distribution,
with 1075 sources located within the central 1 arcmin. We have successfully detected X-ray emissions from 126 out of the 166 known
massive stars of the cluster, and we have collected over 71 000 photons from the magnetar CXO J164710.20-455217.
DERIVATION OF MODIFIED BERNOULLI EQUATION WITH VISCOUS EFFECTS AND TERMINAL V...Wasswaderrick3
In this book, we use conservation of energy techniques on a fluid element to derive the Modified Bernoulli equation of flow with viscous or friction effects. We derive the general equation of flow/ velocity and then from this we derive the Pouiselle flow equation, the transition flow equation and the turbulent flow equation. In the situations where there are no viscous effects , the equation reduces to the Bernoulli equation. From experimental results, we are able to include other terms in the Bernoulli equation. We also look at cases where pressure gradients exist. We use the Modified Bernoulli equation to derive equations of flow rate for pipes of different cross sectional areas connected together. We also extend our techniques of energy conservation to a sphere falling in a viscous medium under the effect of gravity. We demonstrate Stokes equation of terminal velocity and turbulent flow equation. We look at a way of calculating the time taken for a body to fall in a viscous medium. We also look at the general equation of terminal velocity.
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptxMAGOTI ERNEST
Although Artemia has been known to man for centuries, its use as a food for the culture of larval organisms apparently began only in the 1930s, when several investigators found that it made an excellent food for newly hatched fish larvae (Litvinenko et al., 2023). As aquaculture developed in the 1960s and ‘70s, the use of Artemia also became more widespread, due both to its convenience and to its nutritional value for larval organisms (Arenas-Pardo et al., 2024). The fact that Artemia dormant cysts can be stored for long periods in cans, and then used as an off-the-shelf food requiring only 24 h of incubation makes them the most convenient, least labor-intensive, live food available for aquaculture (Sorgeloos & Roubach, 2021). The nutritional value of Artemia, especially for marine organisms, is not constant, but varies both geographically and temporally. During the last decade, however, both the causes of Artemia nutritional variability and methods to improve poorquality Artemia have been identified (Loufi et al., 2024).
Brine shrimp (Artemia spp.) are used in marine aquaculture worldwide. Annually, more than 2,000 metric tons of dry cysts are used for cultivation of fish, crustacean, and shellfish larva. Brine shrimp are important to aquaculture because newly hatched brine shrimp nauplii (larvae) provide a food source for many fish fry (Mozanzadeh et al., 2021). Culture and harvesting of brine shrimp eggs represents another aspect of the aquaculture industry. Nauplii and metanauplii of Artemia, commonly known as brine shrimp, play a crucial role in aquaculture due to their nutritional value and suitability as live feed for many aquatic species, particularly in larval stages (Sorgeloos & Roubach, 2021).
Comparing Evolved Extractive Text Summary Scores of Bidirectional Encoder Rep...University of Maribor
Slides from:
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Track: Artificial Intelligence
https://www.etran.rs/2024/en/home-english/
ESR spectroscopy in liquid food and beverages.pptxPRIYANKA PATEL
With increasing population, people need to rely on packaged food stuffs. Packaging of food materials requires the preservation of food. There are various methods for the treatment of food to preserve them and irradiation treatment of food is one of them. It is the most common and the most harmless method for the food preservation as it does not alter the necessary micronutrients of food materials. Although irradiated food doesn’t cause any harm to the human health but still the quality assessment of food is required to provide consumers with necessary information about the food. ESR spectroscopy is the most sophisticated way to investigate the quality of the food and the free radicals induced during the processing of the food. ESR spin trapping technique is useful for the detection of highly unstable radicals in the food. The antioxidant capability of liquid food and beverages in mainly performed by spin trapping technique.
2. INTRODUCTION
I. The muscular tissue are also known as contractile tissue.
II. Muscles are considered as fleshy part of the body.
III. The ability to contraction,excitation and conductivity of impulse are the characteristics properties of
muscular tissue or muscle.
IV. 40% to 50%of the body weight is considered by muscles.
V. It consist of elongated muscle cells or muscle fibres.
VI. Muscular tissue originate from embryonic mesoderm.
VII. It have no matrix,no power of division and regeneration.
VIII.Study of muscle is known as myology or sarcology.
IX. Muscular tissue is formed of greatly elongated,and highly contractile muscle cells called muscle fibre.
X. Muscle fibres contain contractile units called myofilaments.
XI. Due to modification in general property of protoplasm the cytoplasm in muscle is called sarcoplasm and its
limiting membrane is called sarcolemma.
3. Functions
• It brings about movement of body, parts of the body organs.
• By muscular action it produces body heat.
• It contracts heart and blood vessel.
• Muscles are the agents of brain.
Types of muscle:-
1. Muscles are classified on the basis of their structure and function into three type
2. Striated/striped/skeletal/voluntary/hard muscle.
3. Unstriated/unstriped/nonskeletal/involuntary/smooth muscle
Cardiac muscle.
Striated muscle/striped/skeletal/voluntary:-
These are called striated or striped muscle due to these are thread like structure.
These are mostly attached to the skeleton and hence known as skeletal muscle .
As these muscles are attached to bone hence called as skeletal muscle.
On the basis of contraction and relaxation these are controlled by will so, called voluntary muscle .
These are also hard muscle .
4. The striated muscles are formed of large number of long,unbranched muscles cells or muscle fibres
The length of fibre vary from 1.0 to 40mm and the breadth from 0.01mm to 0.1mm.
A single muscle fibre is surrounded by a sheath of connective tissue known as endomysium.
Bundle of musclefibre form fasciculi which are covered by a sheath of connective tissue known as
perimysium.
Several fasciculi in a muscle is coverd by a sheath of connective tissue called epimysium.
5. Each muscle fibre is cylinderical in shape but may also be spindle,flat irregular shape.
Each myofibril contains nearly 300 light and dark band in one millimeter.
When studied under polarised light the dark band is known as anisotropic or A-band and the light band is
known isotropic or i-band.
6. The I-band is bisected by a thin line, called as z-line or krause’s membrane.
The portion enclosed by two adjacent z- line of a myofibril is considered as contractile unit or sarcomere.
The central portion of A-band has a H-band or Hensen’s disc which is lighter in colour.
In the centre of H-band ,there is a narrow dark line called M-line or M-band(mesophragm) ,where the
myosin filaments are thickened.
The two darker bands of A-band are named as O-band on both the side of Z-line of I-band ,there are thin
darker lines called N-line.
Darker bands contains myosin filaments are 100A0 in diameter .light band contains actin filaments of 50A0 in
diameter .
Myosin filaments are also called thick filament and actin filaments are called thin filament.
7. Actin Filament:-
At regular intervals ,these two filaments are linked together forming an acto-myosin
complex.
MYOSIN + ACTIN → Acto-myosin. ATP
ca++
8. •Actin filament is formed by the actin protein about 25% ,tropomyosin protein about 2 to 10% and small
amount of troponin proteins.
•It is represented by 2 helical strands of globular monomers of G-actin.
•In helical strand G-actins are polymerised to form F-actin filament (fibrous actin filament)
•Each troponin protein is made up of 3 subunit to form troponin complex.
•The troponin complex consists of troponin-C ,a small protein that specifically binds with calcium ion at the
time of muscle contraction ,troponin-I a protin that, binds to both G actin and troponin-C and troponin-I the
largest subunit that binds tropomyosin with other troponin.
9. Mysoin Filament
• Myosin filament are formed of myosin protein molecule(About 50% of myofibril proteins).
• Each myosin protein molecule contains 2 long polypeptide chain with 4 short polypeptide chain.
• Many monomeric proteins called meromyosins.
• Each meromyosin has 2 important parts a globular head with a short arm and a tail former being HMM
(heavy meromyosin) and LMM(light meromyosin).
10. • HMM catalyzes the hydrolysis of ATP and binds to actin.
• LMM lacks ATPase activity and does not combine with actin.
11. MUSCLE CONTRACTION :-
Muscles are contractile in nature. The process by which muscle contract is known as muscle contraction.
Theory regarding muscle contraction is sliding filament theory explained by H.E. Huxley and Hanson.
According to this theory the length of actin and myosin filaments remain constant.
During contraction the length of the A-band remains constant while the length of I-band and H-zone
gradually decreases and finally disappear.
The Z-line touch the end of myosin filament.
The sliding of filaments takes place by means quick formation of crossbridge and their break down . So
that, sarcomere becomes shorter in length as a result of which muscle contract and shorten.
The following condition prevails in the sarcoplasm prior to muscle contraction.
Cross bridges of the myosin heads are oriented at 900 to the actin filaments long axis.
Strong interaction is not possible between these two filaments due to the presence of regulatory proteins
such as troponin.
Troponin –I inhibits the activity of ATPase of myosin heads, while tropomyosin present in the grooves of F-
actin covers the actin binding sites of the myosin heads.
The myosin head contain tightly bound ADP and phosphate molecules.
The concentration of ATP and Mg++ ions in the sarcoplasm is more than the level of calcium ion.
Sarcoplasmic reticulum has higher concentration of calcium ions.
12. There is a cyclic mechanism of contraction and relaxation of a muscle cell. It involves four steps such as ,
A.INITIATION
B.POWER STROKE
C.RELAXATION
D.ENERGY GENERATION
A.INITIATION
The muscle cell contraction is initiated by depolarization of its sarcolemma because of stimulation by nerve
impulse generated by any physical and chemical agents .
The depolarization causes change in the permeability of the sarcoplasmic reticulum to ions .
Rapid diffusion of calcium ions to the sarcoplasm.The level of calcium ions now increases in sarcoplasm to
10-5 M.
Calcium ion binds to troponin-C causing a shift in the position of tropomyosin .
The binding sites on the G-actin are exposed to the actin binding site of myosin heads .so that, the
interaction become stronger .
13. B.POWER STROKE
The myosin head undergoes a conformational change from 900 orientation to 450 causing the actin
filaments to slide about 12nM . This movement of the filament is called power stroke .
This phenomenon is accompanied by release of the bound phosphate and ADP .
Detachment of myosin head causing the restoration of its previous 900 orientation .
Binding of ATP to the myosin head and subsequently the hydrolysis of ATP .
C.RELAXATION
When the nervous stimulation stops ,the sarcolemma is repolarised and the normal permeability of
sacoplasmic reticulum is restored .
This result in the active transport of calcium ions form sarcoplasm to sarcoplasmic reticulum.
So,that reduces the concentration of calcium ions in the sarcoplasm to 10-7M .
This is accomplished by the membrane bound calcium ion pump protein of the reticulum (By the activty of
enzyme ATPase).
The withdrawal of calcium ions make free troponin-C which changes the position of tropomyosin .
14. The tropomyosin comes back to the groove of F-actin which shields the binding sites of G-actin .As a result it
prevents the interaction between the cross bridge of myosin head and actin filament.
D.ENERGY GENERATION
A considerable amount of ATP molecules are consumed during molecular activity .The ultimate source of
ATP is due to the phosphorylation of ADP during glycolysis.
The source of phosphate is phosphor-creatin that is present in the sarcoplasm.
As we know that the globular double head of myosin molecule has two active sites ,one for actin and other
for ATP .The active site for ATP has ATPase activity which splits ATP into ADP+iP
myosin ATPase. Contracting muscle
ATP +H2O→ADP+iP+Energy+Phosphocreatin+ADP -----→ATP+Creatin.
Two molecule of ATP are consumed for each interaction between the cross bridge of myosin head and G-
actin.
One molecule of ATP is required for active transport of each calcium ion from sarcoplasm to sarcoplasmic
reticulum.
16. In summary the mechanism of contraction expressed in the following scheme CONTRACTION-Membrane
depolarization→ca++ released from sarcoplasmic reticulum→myosin ATP are activated→cross bridge
formed→myosin slides along actin
RELAXATION
ca++pumped back into sarcoplasmic reticulum→myosin ATPase is depressed→cross bridge
broken→myosin is pulled back to its resting site
It takes 0.1 sec /contraction .
Muscle fatigue –
By repeated stimulation ,the muscle loose irritability and fails to contract .It is known as muscle fatigue.It
happens due to exahustion of energy and accumulation of lactic acid.
Single twitch-
The single nerve impulse or an electrical shock of sufficient amount brings about contraction in a single
muscle fibre. It is known as muscle twitch.
Rigor mortis-Due to non-availability of ATP ,enzymes,oxygen and food,the muscle remain contracted after
death .It is called rigor mortis
Summation:-When a second stimulus is given to muscle fibre after the 1st one brings about contration.Thus
it adds contraction strength of first stimulus. It is known as summation.
Tetanus:-when a series of stimuli are given to the muscle fibre in a quick succession, the contraction of
muscle fibre continues.The continued state of contraction is known as tetanus.
17. Thresold Stimulus:-
Each Muscle contracts due to some stimulus. The muscle fibre remain relaxed when it is not stimulated.
The specific minimum strength requird for muscle contraction is called as Threshold stimulus.
The stimulus which is unable to bring contraction is called as subliminal stimulus and the stronger stimulus is known as
supraliminal stimulus.
Unstriated/unstriped/Non-Skeletal/Smooth/Non-voluntary muscle:-
i. These muscles are not directly attached to skeleton hence known as non skeletal muscle.
ii. These are connected with visceral organ hence called as visceral muscle.
iii. These are also called smooth, involuntary work will (of ANS) and unstriped.
iv. Each muscle fibre is elongated, spindle shaped tappering at both the ends, length 20 ꜡ to 500 ꜡, breadth 6꜡.
v. Central part is wide.
vi. Uninucleate and nucleus is centric.
vii. Such muscle fibres are less vascular with less mitochondria.
viii. Each muscle fibre contains contractile unit called myofilaments having actin and myosin.
ix. Such type of muscle never fatigue.
x. It takes 0.3sec /contraction.
xi. Absence of dark and light band.
18. Location:-Alimentary canal,blood vessel,lungs,urinary bladder etc.
Function:-Helps in peristalsis, causing slow and prolonged contraction.
Cardiac Muscles:-These are structurally striated and functionally unstriated.
Resembalance with striated muscle:-Cylindrical,vascularised,more mitochondria,Glylogen
granules in sarcoplasm,having light and dark bands.
Resembalance with unstraited muscle:-Uninucleate,involuntary.
19. Own Character:-
i. Branched cardiac muscle fibres are joined with each other by thick junctions called intercalated disc.
ii. Such muscles never fatigue.
iii. Cells attached with each other forming continuous network.
iv. Wave of excitation self generated.
v. Contract quickly powerfully and rhythmically.
vi. It takes 0.8sec/contraction.
20. CONCLUSION
Efficent blood circulation is essentials. Constant supply of food and oxygen . Removal of
waste products. Muscle provides support to bone and other organs. Muscles bring
movement of the body parts and helps in locomotion of an individual. Muscles contracts
heart blood vessels and alimentary canal. Muscle contraction produces heat. Maintains
equilibrium of body. Helps in child birth.