Answer:
a. Five-Carbon Sugar and Phosphate
Explanation:
A nucleotide can be defined as an organic molecule which forms the building block of nucleic acid such as deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
Basically, nucleotide comprises of the following parts;
1. Nitrogenous base: this includes adenine (A), thymine (T), guanine (G), and cytosine (C) which are mainly found in the DNA while adenine (A), guanine (G), uracil (U) and cytosine (C) are found in the RNA.
2. A phosphate group.
3. A penrose sugar: it is either deoxyribose in DNA or ribose in RNA.
The two parts or chemical components of a nucleotide which do not change throughout the structure of DNA are;
I. Five-Carbon Sugar also known as deoxyribose and it has hydrogen on its second carbon.
II. Phosphate: this is the structural backbone that provides support to DNA.
Answer:
Uhhh so here is what I found in the lessons about Principle of Fossil Correlation:
Answer:
The correct answer would be -
Membrane A - Hypotonic solution - the movement of water towards inside the cell
Membrane B - Isotonic soltion - there will be no movement of water
Membrane C - Hyertonic solution - the movement of water towards outside of the cell
Explanation:
This experiment deals with tonicity as this solution will affect the tonicity of the egg membrane. In membrane A there are more solutes inside the cell than outside the cell so it is hypotonic solution so the movement of water will be towards inside the cell.
In membrane B the solutes are equal in both sides so there will be no movement as its isotonic condition while in membrane C the solution is in hypertonic situation as the solutes are more outside than inside.
Thus, the behavior of the membranes are-
Membrane A - Hypotonic solution - the movement of water towards inside the cell
Membrane B - Isotonic soltion - there will be no movement of water
Membrane C - Hyertonic solution - the movement of water towards outside of the cell
The answers are as follows:
1. <span>An inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate: t</span>his is called competitive inhibitor. A competitive inhibitor will compete with the substrate for the active site of the enzyme and bind to the active site, thus incapacitating the substrate from binding to the active site.
2. An inhibitor binds to a site on the enzyme that is not the active site: this is called non competitive inhibitors. Non competitive inhibitors bind to other site in the enzyme which is not the active site of the enzyme. The binding of the inhibitor changes the conformation of the enzyme as well as the active site, thus making it impossible for the substrate to bind to the enzyme effectively.
3. <span>usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity: this is called irreversible or permanent inhibition. Permanent inhibitors form covalent bonds with the enzyme and prevent substrate from binding to the enzyme.
4. T</span><span>he competitive inhibitor competes with the substrate for the ACTIVE SITE on the enzyme: The active site of an enzyme is the place where the substrate normally bind in order to activate a enzyme. Competitive inhibitors are those inhibitors that compete with the substrate for the active site of the enzyme and prevent the substrate from binding there.
5. W</span><span>hen the noncompetitive inhibitor is bonded to the enzyme, the shape of the ENZYME is distorted. The non competitive inhibitors are those inhibitors that bind to other places in the enzyme instead of the active site. The binding of the non competitive inhibitor usually distort the shape and the conformation of the enzyme thus preventing the substrate from binding to it effectively.
6. E</span><span>nzyme inhibitors disrupt normal interactions between an enzyme and its SUBSTRATE. The principal function of enzyme inhibitor is to prevent the substrate from binding to the appropriate enzyme. This is usually done in the human system in order to regulate the activities of enzymes.</span>
