Name the four types of protein and gives their function
Answers
Answer:
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Explanation:
Primary Structure. Primary Structure describes the unique order in which amino acids are linked together to form a protein. ...
Secondary Structure. Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape. ...
Tertiary Structure. ...
Quaternary Structure.
Answer:
Explanation:
1. Primary Structure
Primary Structure describes the unique order in which amino acids are linked together to form a protein. Proteins are constructed from a set of 20 amino acids. Generally, amino acids have the following structural properties:
A carbon (the alpha carbon) bonded to the four groups below:
A hydrogen atom (H)
A Carboxyl group (-COOH)
An Amino group (-NH2)
A "variable" group or "R" group
All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and an amino group. The "R" group varies among amino acids and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular genetic code. The order of amino acids in a polypeptide chain is unique and specific to a particular protein. Altering a single amino acid causes a gene mutation, which most often results in a non-functioning protein.
2. Secondary Structure
Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape. There are two types of secondary structures observed in proteins. One type is the alpha (α) helix structure. This structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet. This structure appears to be folded or pleated and is held together by hydrogen bonding between polypeptide units of the folded chain that lie adjacent to one another.
3. Tertiary Structure
Tertiary Structure refers to the comprehensive 3-D structure of the polypeptide chain of a protein. There are several types of bonds and forces that hold a protein in its tertiary structure.
Hydrophobic interactions greatly contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will seek contact with their aqueous environment, while amino acids with hydrophobic "R" groups will seek to avoid water and position themselves towards the center of the protein.
Hydrogen bonding in the polypeptide chain and between amino acid "R" groups helps to stabilize protein structure by holding the protein in the shape established by the hydrophobic interactions.
Due to protein folding, ionic bonding can occur between the positively and negatively charged "R" groups that come in close contact with one another.
Folding can also result in covalent bonding between the "R" groups of cysteine amino acids. This type of bonding forms what is called a disulfide bridge. Interactions called van der Waals forces also assist in the stabilization of protein structure. These interactions pertain to the attractive and repulsive forces that occur between molecules that become polarized. These forces contribute to the bonding that occurs between molecules.
4. Quaternary Structure
Quaternary Structure refers to the structure of a protein macromolecule formed by interactions between multiple polypeptide chains. Each polypeptide chain is referred to as a subunit. Proteins with quaternary structure may consist of more than one of the same type of protein subunit. They may also be composed of different subunits. Hemoglobin is an example of a protein with quaternary structure. Hemoglobin, found in the blood, is an iron-containing protein that binds oxygen molecules. It contains four subunits: two alpha subunits and two beta subunits.