Convert 24 hours into minutes
24 hours = 1440 minutes
Divide 1440 by 15
There’s 96 divisions
Now take 2^96 power
You will have 7.9 x 10^28 bacteria
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 Sahel. The Sahel is a region of sub-Saharan Africa and it is also a zone of ecological transition between the Sahara to the north and the wetter savannas to the south. Sahel belt or Sahel is a tropical savanna ecoregion in Africa. Africa is the second largest continent. It has 54 sovereign countries.
Ingestion is the process of obtaining food that requires specialized mouthparts
Answer:
The ribosomes on the rough endoplasmic reticulum (RER) most likely produces neuronal special proteins.
Explanation:
Conduction of electrical impulses by action potentials of neurons takes place through controlled flow of charged ions through neuronal membranes. This ion transfer is controlled by specialized neuronal channel proteins which are present in the neuronal cell membrane.
These channel proteins allow for hydrophillic passage of ions and water molecules across the neuronal membranes.
Ribosomes that are attached to the RER are involved in protein synthesis. They carry the code for proteins carried by the mRNA and translate into respective protein.
The RER along with some free ribosomes cluster together as Nissl bodies and are mainly involved in neuronal specialized proteins.
