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Yes it does. It also commonly contains quaternary structure.
Secondary structure refers to folding and bonding interactions between atoms of the polypeptide backbone, either forming alpha-helices or Beta-sheets. Oxytocin contains both of these secondary structures as well as Beta-turns. Beta-sheets come in anti-parallel and parallel versions. Parallel means that the direction of the associated chains run in the same direction; N-terminus to C-terminus. Anti-parallel means that one or more of the associated chains run in an opposite direction to the others.
Tertiary structure refers to interactions between side chains of the polypeptide residues. a good example of this is the disulfide bonds liking two cysteine residues which does occur in Oxytocin.
Quaternary structure refers to association of separate polypeptide chains. Oxytocin can be found as a single chain in which case there is no quaternary structure. It is not uncommon however to find it as a pentamer, tetramer, or dimer. Conditions play a major factor in effecting its quaternary structure. whether it is in aqueous solution, biological conditions (cells), or crystallized. Another good example of quaternary structure is Hemoglobin. Hemoglobin is a dimer of dimers. 2 alpha-globin chains and 2 beta-globin chains.
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What is it called when a protein folds back onto itself?
a. tertiary structure b. primary structure c. secondary structure d. tertiary structure pick your best answer
What does the tertiary structure of a protein tell you about the protein?
The tertiary structure of a protein provides information about how its secondary structural elements (such as alpha helices and beta sheets) are arranged in three dimensions to form a functional protein. It also reveals the specific interactions between amino acid residues and the overall 3D shape of the protein, which are crucial for its function. Additionally, the tertiary structure can give insight into the protein's stability, ligand binding sites, and biological activity.
What is the tertiary structure for a protein?
'The Quaternary structure of a protein is the 4th level of folding for a protein. An example of this would be a red blood cell, which is a quaternary structure, it is made up of alpha helicies and also beta pleated in the tertiary structure. The Quaternary structure of a protein contains 4 tertiary structures in it.
Which structure would probably not be affected when a protein is denatured?
The primary structure of a protein, which is the sequence of amino acids, would not be affected when a protein is denatured. Denaturation typically involves disruption of the higher-order structures such as secondary, tertiary, and quaternary structures.
What are the different stages of folding?
Primary structure: The linear sequence of amino acids in a protein. Secondary structure: Formation of alpha helices and beta sheets through hydrogen bonding. Tertiary structure: 3D folding of the secondary structures into a unique overall shape. Quaternary structure: Assembly of multiple folded protein subunits to form a functional protein complex.
