The proteins that comprise the myofibril, including actin and myosin and several more. The myofibrillar protein components most important for muscle fiber structure are actin and myosin. They are the most abundant proteins in muscle and are directly involved in the ability of muscle to contract and to relax.
The different levels of protein structure are known as primary, secondary, tertiary, and quaternary structure. The primary structure is the sequence of amino acids that make up a polypeptide chain.
Primary Structure of Proteins
-The primary structure is the sequence of amino acids that make up a polypeptide chain. 20 different amino acids are found in proteins. The exact order of the amino acids in a specific protein is the primary sequence for that protein.
Secondary Structure of Proteins
-Protein secondary structure refers to regular, repeated patterns of folding of the protein backbone. The two most common folding patterns are the alpha helix and the beta sheet.
Alpha Helix
-In an alpha helix, the polypeptide backbone coils around an imaginary helix axis in clockwise direction.
In this illustration, only the N-C-CO backbone atoms are shown. Note the coiling of the backbone around an imaginary axis down the center of the helix.
Beta sheet
-In the beta sheet secondary structure, the polypeptide backbone is nearly fully extended. The R-groups (not shown) are alternately pointed above and then below the extended backbone.
Tertiary Structure of Proteins
-Tertiary structure refers to the overall folding of the entire polypeptide chain into a specific 3D shape. The tertiary structure of enzymes is often a compact, globular shape.
Quaternary Structure of Proteins
-Many proteins are formed from more than one polypeptide chain. The quaternary structure describes the way in which the different subunits are packed together to form the overall structure of the protein. For example, the human hemoglobin molecule shown below is made of four subunits.
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Answer:
The proteins that comprise the myofibril, including actin and myosin and several more. The myofibrillar protein components most important for muscle fiber structure are actin and myosin. They are the most abundant proteins in muscle and are directly involved in the ability of muscle to contract and to relax.
The different levels of protein structure are known as primary, secondary, tertiary, and quaternary structure. The primary structure is the sequence of amino acids that make up a polypeptide chain.
Primary Structure of Proteins
-The primary structure is the sequence of amino acids that make up a polypeptide chain. 20 different amino acids are found in proteins. The exact order of the amino acids in a specific protein is the primary sequence for that protein.
Secondary Structure of Proteins
-Protein secondary structure refers to regular, repeated patterns of folding of the protein backbone. The two most common folding patterns are the alpha helix and the beta sheet.
Alpha Helix
-In an alpha helix, the polypeptide backbone coils around an imaginary helix axis in clockwise direction.
In this illustration, only the N-C-CO backbone atoms are shown. Note the coiling of the backbone around an imaginary axis down the center of the helix.
Beta sheet
-In the beta sheet secondary structure, the polypeptide backbone is nearly fully extended. The R-groups (not shown) are alternately pointed above and then below the extended backbone.
Tertiary Structure of Proteins
-Tertiary structure refers to the overall folding of the entire polypeptide chain into a specific 3D shape. The tertiary structure of enzymes is often a compact, globular shape.
Quaternary Structure of Proteins
-Many proteins are formed from more than one polypeptide chain. The quaternary structure describes the way in which the different subunits are packed together to form the overall structure of the protein. For example, the human hemoglobin molecule shown below is made of four subunits.
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