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>
Below are the choices that can be found elsewhere:
a.66 s
<span>b.68 s </span>
<span>c.70 s </span>
<span>d.78 s
</span>
<span>An outlier is a result that is abnormally too high or too low. Most of the results fall between 66 and 70, but 78 seems to be abnormal, so it's your outlier. The answer is D. Hope it helps :)</span>
The answer is 1000 kilocarolies. It is important to keep in mind that Energy is passed up the food chain from one trophic level to the next but a lot of it is lost along the way. Energy is passed up the food chain from one trophic level to the next. However, only about 10% of the total energy stored in organisms at one trophic level is actually transferred to organisms at the next trophic level. Therefore; if the producers have 1 million kilocarolies, then the energy transferred to the primary consumer will be 100,000 kilocalories (10% of a million), and the energy transferred to the secondary consumer will be 10,000 kilocalories (10% of 100,000) and the energy to the tertiary consumer will be 1000 kilocarolies (10% of 10,000).
The lithosphere is carried on a softer, but still firm, layer of rock called the asthenosphere. The ashenosphere is <span>the upper layer of the earth's mantle, below the lithosphere, in which there is relatively low resistance to plastic flow and convection is thought to occur.</span>
