This type of mutation would be called a deletion
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Answer: His genes contain a mutation that prevents red blood cells from proper functioning.
Explanation:
Hereditary anaemia is a type of disorder that are genetically transmitted to the offsprings by the parents . These type of anaemia are inherited from the parent including sickle cell anaemia.
The offsprings inherent Gene mutation that cause abnormalitiies. They inherit abnormal haemoglobin that can reduce the life span of red blood cells thereby affecting their proper functioning of carrying oxygen in the blood, leading to anaemia.
<span>Heat strokeHeat stroke is a condition caused by failure of the body's temperature-regulating mechanism when exposed to high temperatures. Heat stroke is treated by keeping the body temperature less than 102.5°F. Various cooling methods includes removing clothing, placing the patient in front of a large fan, and immersing the patient into a tub of cool water.
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<u>ANSWER:</u>
The correct option is A: They transport heat over long distances affecting the wind that blows over the land.
<u>EXPLANATION:</u>
- Ocean currents carry cool or warm water or currents over long distances thereby affecting the wind that blows over the place bringing about a change in the climate.
- When the ocean currents carry cool air, the warm wind gets displaced by the cool air and therefore the climate of the place becomes cold.
- When the ocean currents carry warm air or water, the climate of the place becomes warmer.
- By transporting hot or cold currents, the ocean currents affect the climatic conditions of land and so bring about a change of weather.
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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