Help with Sarcomere Physiology - Anatomy
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Where within the sarcomere is myosin contained?
Where within the sarcomere is myosin contained?
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Thick filaments contain myosin. Thick filaments are present in the A band in the center of the sarcomere. Myosin has six polypeptide chains, including one pair of heavy chains and two pair if light chains. Each myosin molecule has two “heads” attached to a single “tail.” The myosin heads are capable of ATP hydrolysis and bind ATP and actin, and are involved in cross bridge formation.
Thick filaments contain myosin. Thick filaments are present in the A band in the center of the sarcomere. Myosin has six polypeptide chains, including one pair of heavy chains and two pair if light chains. Each myosin molecule has two “heads” attached to a single “tail.” The myosin heads are capable of ATP hydrolysis and bind ATP and actin, and are involved in cross bridge formation.
Which of the following sarcomere portions does not decrease in length during muscular contraction?
Which of the following sarcomere portions does not decrease in length during muscular contraction?
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During muscular contraction, the myosin heads pull the actin filaments toward one another resulting in a shortened sarcomere. While the I band and H zone will disappear or shorten, the A band length will remain unchanged. This is because the A band corresponds to the full length of the myosin filament, or thick filament. Since the myosin filament does not actually change length, the A band remains constant.
The I band corresponds to the region of action that does not overlap with myosin. The length of the actin filament does not change during contraction, but the region of overlap increases. This results in a decrease of the non-overlapped I band.
The H zone refers to the region of myosin that is not overlapped by action. As the region of overlap grows, the H zone shrinks.
During muscular contraction, the myosin heads pull the actin filaments toward one another resulting in a shortened sarcomere. While the I band and H zone will disappear or shorten, the A band length will remain unchanged. This is because the A band corresponds to the full length of the myosin filament, or thick filament. Since the myosin filament does not actually change length, the A band remains constant.
The I band corresponds to the region of action that does not overlap with myosin. The length of the actin filament does not change during contraction, but the region of overlap increases. This results in a decrease of the non-overlapped I band.
The H zone refers to the region of myosin that is not overlapped by action. As the region of overlap grows, the H zone shrinks.
An investigational drug prevents skeletal muscle contraction by preventing ATP hydrolysis at the active site in muscle tissue. Where is this drug most likely to act?
An investigational drug prevents skeletal muscle contraction by preventing ATP hydrolysis at the active site in muscle tissue. Where is this drug most likely to act?
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ATP binds to myosin head regions and is hydrolyzed to ADP and inorganic phosphate when muscle relaxes. The release of these products allows the contraction to occur as the myosin head changes position. The binding of new ATP releases the myosin head from actin, and allows the muscle to relax prior to another round of hydrolysis. This explains why, in the absence of adequate ATP, muscle can remain in a contracted state. This phenomenon, when seen in the deceased, is called rigor mortis.
ATP binds to myosin head regions and is hydrolyzed to ADP and inorganic phosphate when muscle relaxes. The release of these products allows the contraction to occur as the myosin head changes position. The binding of new ATP releases the myosin head from actin, and allows the muscle to relax prior to another round of hydrolysis. This explains why, in the absence of adequate ATP, muscle can remain in a contracted state. This phenomenon, when seen in the deceased, is called rigor mortis.
Ions are key in mediating muscle contraction. Which of the following structures interacts directly with ions to expose actin binding sites in contracting muscle?
Ions are key in mediating muscle contraction. Which of the following structures interacts directly with ions to expose actin binding sites in contracting muscle?
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Troponin (also called troponin C) is the most direct structure that interacts with ions involved in initiating muscle contractions. Once bound to calcium ions, troponin facilitates the movement of tropomyosin away from actin binding sites, allowing myosin to bind and, ultimately, contract. Without the binding of calcium ions to troponin, the myosin-binding site on actin remains obscured by tropomyosin and contraction cannot occur.
Troponin (also called troponin C) is the most direct structure that interacts with ions involved in initiating muscle contractions. Once bound to calcium ions, troponin facilitates the movement of tropomyosin away from actin binding sites, allowing myosin to bind and, ultimately, contract. Without the binding of calcium ions to troponin, the myosin-binding site on actin remains obscured by tropomyosin and contraction cannot occur.
In excitation-contraction coupling in skeletal muscle, the calcium released from the smooth endoplasmic reticulum binds to which of the following?
In excitation-contraction coupling in skeletal muscle, the calcium released from the smooth endoplasmic reticulum binds to which of the following?
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When calcium is released in muscle cells, it binds to troponin. This binding allows tropomyosin to change its orientation, exposing the myosin-binding sites on actin. Myosin heads can then bind to actin, and contraction can occur.
Calmodulin is a molecule that can bind calcium; however, it plays important roles in cell signal cascades and is not involved in skeletal muscle contraction.
When calcium is released in muscle cells, it binds to troponin. This binding allows tropomyosin to change its orientation, exposing the myosin-binding sites on actin. Myosin heads can then bind to actin, and contraction can occur.
Calmodulin is a molecule that can bind calcium; however, it plays important roles in cell signal cascades and is not involved in skeletal muscle contraction.
In a muscle cell, the H-zone has .
In a muscle cell, the H-zone has .
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The H-zone is an area made up of only thick filaments (myosin). The I-band is thin filaments (actin) only, and the A-band is where there are thick and thin filaments. The Z-disc is dividing feature between sarcomeres and appears as dark lines in electron micrographs.
The H-zone is an area made up of only thick filaments (myosin). The I-band is thin filaments (actin) only, and the A-band is where there are thick and thin filaments. The Z-disc is dividing feature between sarcomeres and appears as dark lines in electron micrographs.
During muscle contraction, which band(s) of the sarcomere shorten(s)?
During muscle contraction, which band(s) of the sarcomere shorten(s)?
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Muscle contraction results in both the H-band and I-bands shortening, but the A-band remains the same length (A band is Always the same). The Z-band is a static structure and doesn't change size.
Muscle contraction results in both the H-band and I-bands shortening, but the A-band remains the same length (A band is Always the same). The Z-band is a static structure and doesn't change size.
Troponin binds with which ion?
Troponin binds with which ion?
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Troponin is the regulatory protein that permits cross bridge formation when it binds 
. Troponin is a complex of three globular proteins. Troponin C (
) is the 
binding protein, that when bound to 
, permits the interaction of actin and myosin via conformational change that reveals the myosin binding site on actin, and thus muscular contraction.
Troponin is the regulatory protein that permits cross bridge formation when it binds
Where can you find a ryanodine receptor?
Where can you find a ryanodine receptor?
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The ryanodine receptor is a calcium channel that is responsible for the release of calcium ions. It is located in the sarcoplasmic reticulum. The release of calcium is a required step in muscle contraction. The ryanodine receptor pumps calcium ions from the intracellular fluid into the interior of the sarcoplasmic reticulum, this process keeps the intracellular calcium ions low and creates a concentration gradient.
The ryanodine receptor is a calcium channel that is responsible for the release of calcium ions. It is located in the sarcoplasmic reticulum. The release of calcium is a required step in muscle contraction. The ryanodine receptor pumps calcium ions from the intracellular fluid into the interior of the sarcoplasmic reticulum, this process keeps the intracellular calcium ions low and creates a concentration gradient.
Muscle myofibrils are arranged longitudinally into sarcomeres. Which of the following correctly lists the boundaries of a single sarcomere?
Muscle myofibrils are arranged longitudinally into sarcomeres. Which of the following correctly lists the boundaries of a single sarcomere?
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Each myofibril contains interdigitating thick and thin filaments arranged longitudinally in sarcomeres. Repeating units of sarcomeres account for the unique banding pattern in striated muscle. A sarcomere runs from Z line to Z line.
Each myofibril contains interdigitating thick and thin filaments arranged longitudinally in sarcomeres. Repeating units of sarcomeres account for the unique banding pattern in striated muscle. A sarcomere runs from Z line to Z line.
Which specific protein of troponin is responsible for attaching the troponin complex to tropomyosin?
Which specific protein of troponin is responsible for attaching the troponin complex to tropomyosin?
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Troponin is a complex of three globular regulatory proteins (T, C, and I). Troponin is essential to the contraction of skeletal and cardiac muscle, but is not involved in the contraction of smooth muscle. Troponin T (think of: T for tropomyosin) binds to tropomyosin creating the troponin-tropomyosin complex, which helps to position tropomyosin onto actin. Troponin I (think of I for inhibition) binds actin, holding the actin-tropomyosin complex in place. This inhibits the myosin heads from binding their binding sites on actin. Lastly, troponin C (think of C for calcium) is responsible for binding calcium. This step is allows for the interaction of actin and myosin, thus activating the muscle for contraction.
Troponin is a complex of three globular regulatory proteins (T, C, and I). Troponin is essential to the contraction of skeletal and cardiac muscle, but is not involved in the contraction of smooth muscle. Troponin T (think of: T for tropomyosin) binds to tropomyosin creating the troponin-tropomyosin complex, which helps to position tropomyosin onto actin. Troponin I (think of I for inhibition) binds actin, holding the actin-tropomyosin complex in place. This inhibits the myosin heads from binding their binding sites on actin. Lastly, troponin C (think of C for calcium) is responsible for binding calcium. This step is allows for the interaction of actin and myosin, thus activating the muscle for contraction.
During muscle contraction, which band(s) of the sarcomere shorten(s)?
During muscle contraction, which band(s) of the sarcomere shorten(s)?
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Muscle contraction results in both the H-band and I-bands shortening, but the A-band remains the same length (A band is Always the same). The Z-band is a static structure and doesn't change size.
Muscle contraction results in both the H-band and I-bands shortening, but the A-band remains the same length (A band is Always the same). The Z-band is a static structure and doesn't change size.
Which of the following sarcomere portions does not decrease in length during muscular contraction?
Which of the following sarcomere portions does not decrease in length during muscular contraction?
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During muscular contraction, the myosin heads pull the actin filaments toward one another resulting in a shortened sarcomere. While the I band and H zone will disappear or shorten, the A band length will remain unchanged. This is because the A band corresponds to the full length of the myosin filament, or thick filament. Since the myosin filament does not actually change length, the A band remains constant.
The I band corresponds to the region of action that does not overlap with myosin. The length of the actin filament does not change during contraction, but the region of overlap increases. This results in a decrease of the non-overlapped I band.
The H zone refers to the region of myosin that is not overlapped by action. As the region of overlap grows, the H zone shrinks.
During muscular contraction, the myosin heads pull the actin filaments toward one another resulting in a shortened sarcomere. While the I band and H zone will disappear or shorten, the A band length will remain unchanged. This is because the A band corresponds to the full length of the myosin filament, or thick filament. Since the myosin filament does not actually change length, the A band remains constant.
The I band corresponds to the region of action that does not overlap with myosin. The length of the actin filament does not change during contraction, but the region of overlap increases. This results in a decrease of the non-overlapped I band.
The H zone refers to the region of myosin that is not overlapped by action. As the region of overlap grows, the H zone shrinks.
An investigational drug prevents skeletal muscle contraction by preventing ATP hydrolysis at the active site in muscle tissue. Where is this drug most likely to act?
An investigational drug prevents skeletal muscle contraction by preventing ATP hydrolysis at the active site in muscle tissue. Where is this drug most likely to act?
Tap to see back →
ATP binds to myosin head regions and is hydrolyzed to ADP and inorganic phosphate when muscle relaxes. The release of these products allows the contraction to occur as the myosin head changes position. The binding of new ATP releases the myosin head from actin, and allows the muscle to relax prior to another round of hydrolysis. This explains why, in the absence of adequate ATP, muscle can remain in a contracted state. This phenomenon, when seen in the deceased, is called rigor mortis.
ATP binds to myosin head regions and is hydrolyzed to ADP and inorganic phosphate when muscle relaxes. The release of these products allows the contraction to occur as the myosin head changes position. The binding of new ATP releases the myosin head from actin, and allows the muscle to relax prior to another round of hydrolysis. This explains why, in the absence of adequate ATP, muscle can remain in a contracted state. This phenomenon, when seen in the deceased, is called rigor mortis.
Ions are key in mediating muscle contraction. Which of the following structures interacts directly with ions to expose actin binding sites in contracting muscle?
Ions are key in mediating muscle contraction. Which of the following structures interacts directly with ions to expose actin binding sites in contracting muscle?
Tap to see back →
Troponin (also called troponin C) is the most direct structure that interacts with ions involved in initiating muscle contractions. Once bound to calcium ions, troponin facilitates the movement of tropomyosin away from actin binding sites, allowing myosin to bind and, ultimately, contract. Without the binding of calcium ions to troponin, the myosin-binding site on actin remains obscured by tropomyosin and contraction cannot occur.
Troponin (also called troponin C) is the most direct structure that interacts with ions involved in initiating muscle contractions. Once bound to calcium ions, troponin facilitates the movement of tropomyosin away from actin binding sites, allowing myosin to bind and, ultimately, contract. Without the binding of calcium ions to troponin, the myosin-binding site on actin remains obscured by tropomyosin and contraction cannot occur.
In excitation-contraction coupling in skeletal muscle, the calcium released from the smooth endoplasmic reticulum binds to which of the following?
In excitation-contraction coupling in skeletal muscle, the calcium released from the smooth endoplasmic reticulum binds to which of the following?
Tap to see back →
When calcium is released in muscle cells, it binds to troponin. This binding allows tropomyosin to change its orientation, exposing the myosin-binding sites on actin. Myosin heads can then bind to actin, and contraction can occur.
Calmodulin is a molecule that can bind calcium; however, it plays important roles in cell signal cascades and is not involved in skeletal muscle contraction.
When calcium is released in muscle cells, it binds to troponin. This binding allows tropomyosin to change its orientation, exposing the myosin-binding sites on actin. Myosin heads can then bind to actin, and contraction can occur.
Calmodulin is a molecule that can bind calcium; however, it plays important roles in cell signal cascades and is not involved in skeletal muscle contraction.
In a muscle cell, the H-zone has .
In a muscle cell, the H-zone has .
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The H-zone is an area made up of only thick filaments (myosin). The I-band is thin filaments (actin) only, and the A-band is where there are thick and thin filaments. The Z-disc is dividing feature between sarcomeres and appears as dark lines in electron micrographs.
The H-zone is an area made up of only thick filaments (myosin). The I-band is thin filaments (actin) only, and the A-band is where there are thick and thin filaments. The Z-disc is dividing feature between sarcomeres and appears as dark lines in electron micrographs.
Where within the sarcomere is myosin contained?
Where within the sarcomere is myosin contained?
Tap to see back →
Thick filaments contain myosin. Thick filaments are present in the A band in the center of the sarcomere. Myosin has six polypeptide chains, including one pair of heavy chains and two pair if light chains. Each myosin molecule has two “heads” attached to a single “tail.” The myosin heads are capable of ATP hydrolysis and bind ATP and actin, and are involved in cross bridge formation.
Thick filaments contain myosin. Thick filaments are present in the A band in the center of the sarcomere. Myosin has six polypeptide chains, including one pair of heavy chains and two pair if light chains. Each myosin molecule has two “heads” attached to a single “tail.” The myosin heads are capable of ATP hydrolysis and bind ATP and actin, and are involved in cross bridge formation.
Troponin binds with which ion?
Troponin binds with which ion?
Tap to see back →
Troponin is the regulatory protein that permits cross bridge formation when it binds . Troponin is a complex of three globular proteins. Troponin C () is the binding protein, that when bound to , permits the interaction of actin and myosin via conformational change that reveals the myosin binding site on actin, and thus muscular contraction.
Troponin is the regulatory protein that permits cross bridge formation when it binds
Where can you find a ryanodine receptor?
Where can you find a ryanodine receptor?
Tap to see back →
The ryanodine receptor is a calcium channel that is responsible for the release of calcium ions. It is located in the sarcoplasmic reticulum. The release of calcium is a required step in muscle contraction. The ryanodine receptor pumps calcium ions from the intracellular fluid into the interior of the sarcoplasmic reticulum, this process keeps the intracellular calcium ions low and creates a concentration gradient.
The ryanodine receptor is a calcium channel that is responsible for the release of calcium ions. It is located in the sarcoplasmic reticulum. The release of calcium is a required step in muscle contraction. The ryanodine receptor pumps calcium ions from the intracellular fluid into the interior of the sarcoplasmic reticulum, this process keeps the intracellular calcium ions low and creates a concentration gradient.