The name of the structures that some protists form to move are flagella, which are like long moving hairs.
Answer:
The paramecium body.
Explanation:
1. The objective lenses on a compound light microscope doess have powers that start of as smallest to highest power, 4x, 10x, and 40x on the maximum power setting. This means that the sample can be magnified either, 40x, 100x or 400x.
At 40x magnification Stella will see organism 5mm.
At 100x magnification Stella will be able to see organism 2mm.
At 400x magnification Stella will be able to see organism more closely, 0.45mm, or 450 microns.
2. Paramecia are shoe shape or molded and almost transparent and shrouded in a defensive pellicle.
Pellicle capacities like skin and shields them from the components. For movement they have cilia.
Answer:
(B) open stomata only at night, limiting water loss because of heat and low humidity.
Explanation:
CAM plants are found in the regions characterized by very hot and dry environmental conditions. These plants reduce the water loss through transpiration by exhibiting CAM photosynthesis.
They open the stomata during night time when the air is cooler and rich in moisture. They take in CO2 during night time and fix it into the oxaloacetate which in turn is converted into malate and is stored in the vacuoles.
During day time, stomata remain closed to prevent water loss and the CO2 trapped during night time (released by decarboxylation of malate) enter the Calvin cycle.
The answer is; warming of ocean water in the east of the Pacific Ocean close to the western coasts of South America.
The warming of the oceanic waters causes a current that pushes the warm waters eastwards of the Pacific Ocean at the equator. This counters and overpowers the prevailing trade winds that blow westwards. The currents bring in storms on the West coast of South America as the currents exchange heat with the atmosphere .
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>
