Tertiary Structure<span> - refers to the comprehensive 3-D structure of the polypeptide chain of a </span>protein<span>. There are several types of bonds and forces that hold a protein in its tertiary structure. </span>Hydrophobic interactions<span> 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. </span>Hydrogen bonding<span> 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, </span>ionic bonding<span> 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 </span>disulfide bridge<span>. </span>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. <span>All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and amino group. The </span>"R" group<span> varies among </span>amino acids<span> and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular</span>genetic code<span>. The order of amino acids in a polypeptide chain is unique and specific to a particular protein. Altering a single amino acid causes a </span>gene mutation, which most often results in a non-functioning protein.
<span>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.
</span><span>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.
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The hydrogen molecules in water keep it together
Answer:
Fungi
Explanation:
Because they have obvious similarities with plants.
both Fungi and plants are immobile , have cell wall and grow in soil.
The correct option is B.
An alteration in an individual's gene may either be beneficial or detrimental. If the alteration in the gene sequence confers a genetic advantage on the individual then the alteration is beneficial but it the alteration confers a genetic disadvantage on the individual, then the alteration is detrimental.
Yes, the wings are vestigial structures because they are still apart of the birds' bodies but they can't use them for flight. The article says it's because of a genetic mutation.
