The best thing to do is this:
the subjects in the experimental group should be given large, daily dose of vitamin C while the control group subjects should be given a daily dose of sugar pills that are disguised as vitamin C.
The research can then observe the differences between the two groups.
I believe i the correct answer is c because he notices that some of the traits weren't being passed on.
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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>
The answer would be Four.
Answer:
The amphipathic property of the phospholipids that constitute the membrane
Explanation:
It seems like a options-based answer so it would be better if they were included here but basically, each of those phospholipid molecules has two parts with antagonistic reactions towards water.
The head is polar or hydrophilic, wich means it can be sorrounded by water. The tail, is apolar or hydrophobic which means it is repelled by water.
The interior and exterior of the cell is contain water-based substances, that's why the heads of the phospholipids are oriented like that with the tails protected inside the membrane.
This double layer structure has a fundamental role in the fluid property of the cell membrane from which derive most of it's functions.