<span>Let's consider a scenario in which the resting membrane potential changes from −70 mV to +70 mV, but the concentrations of all ions in the intracellular and extracellular fluids are unchanged. Predict how this change in membrane potential affects the movement of Na+. The electrical gradient for Na+ would tend to move Na+ Outside the cell (extracellular) while the chemical gradient for Na+ would tend to move Na+ Inside the cell (intracellular).
The electrical gradient is defined as the + goes to the - and the - goes to the +
Na + has a positive charge, but there's more positive charge inside the cell than outside (due to potassium), therefore, Na+ goes extracellular (out)
The concentration gradient considers that the ion will go from the most concentrated to at least concentrated by passive diffusion so no trans-membrane proteins in the game attention.Na + is very concentrated in extracellular and few intracellular, therefore, it tends to go intracellular (in).</span>
Answer:
There was a time when I was in high school and I had a Math test. I did all the tasks in the test and was sure I answered everything correctly. However, just before I was about to submit the test, I saw that I forgot to add the minus sign (-) in one of the results. I quickly corrected my mistake and successfully submitted my test. In the end, I got an A as I really answered everything correctly.
Answer:
C
Explanation:
Small objects usually do not permeate the surface of the water due to its high tension. The covalent bonding of water allows for its unique ability of high surface tension.
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>
