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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Generally nonsense is much much worse. It creates a premature stop code which can throw off the entire chain of codons and makes things much much worse. A good way to remember this is that the nonsense mutations make the codons not make sense.
Answer:
90 percent
Explanation:
Based on average estimated juvenile and adult survival rate for each species
Answer:
he relationship between environment, variation and selection lay the foundation for natural selection and evolution.
Genetic variations are present among species due to number of reasons like recombination or crossing over during meiosis, mutations, random fertilization etc. These factors bring changes among the members of a species. Some of the species become better adapted to survive in a particular environment whereas some are not better adapted and become extinct over a period of time. The environment selects the organisms that are best adapted to survive and hence lead to variations.
Explanation:
here is you anserw please rate me the most branilest
The answer is diffusion.
The most important mechanism that enables oxygen and carbon dioxide (but as well other small molecules such as glucose, amino acids, wastes) across capillary walls is diffusion. Diffusion is a net movement of molecules through some barrier from an area of high concentration to the area of low concentration. When blood rich in oxygen reaches capillaries close to the cell, now there <span>is </span>more oxygen in the capillaries than in the cells and by diffusion, oxygen will pass capillary walls and enter the cell. Since blood in capillaries lacks in carbon dioxide, it will easily leave the cells and enter the blood. It should be taken into consideration that capillary walls may be fenestrated, continuous, and discontinuous which can affect movement through them.
