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When a skeletal muscle contracts a protein called a myosin hooks onto pulls against a partner protein called?
When a skeletal muscle contracts, a protein called a myosin hooks onto and pulls against a "partner" protein calledA. actin.B. a sarcoplasm.C.myofibril.D. a sarcomere.the answer is A actin
What protein makes up the thick myofilament?
The protein that makes up the thick myofilament in muscle cells is called myosin. Myosin is a motor protein that plays a key role in muscle contraction by interacting with actin, the protein in the thin myofilament.
What are the thick protein filaments in the cell made of?
The thick protein filaments in a cell are primarily made of a protein called myosin. Myosin filaments are involved in muscle contraction and various other cellular processes such as cell motility and cytokinesis.
Does protein make actin and myosin?
Actin and myosin are proteins. Protein is a broad category of molecules.
What are the myofilaments called in a muscle cell?
The myofilaments in a muscle cell are called actin and myosin. Actin and myosin are protein filaments that work together during muscle contraction to generate force and movement.
What are thick myofilaments of muscles called?
Actin. Myosin are the thin ones.... it's actually the reverseThe thin filaments are composed primarily by the protein Actin.The thick filaments are composed primarily of the protein Myosin.
The larger of the two filaments forming a cross-bridge is made of a protein called?
Myosin
Is it true that thick filaments are made of a protein called actin?
false, it's made of myosin
Which proteins found myofilaments contains the cross bridge?
The two muscle filaments are Myosin and Actin. Myosin is the thicker of the two. When a muscle contracts, a hook like particle extends off the myosin and grabs the actin pulling it in causing the contraction/ tension of the muscle
What Protein found in skeletal muscle?
myosin
What are the contractile protein of muscle?
Actin and Myosin
What is the chemical makeup of actin and myosin?
Protein.
