Because the interior of the lipid bilayer contains the nonpolar _____molecules__________, only small nonpolar substances are able to diffuse directly across the cell membrane
Answer:
Hydrogen Bonding in Water (1) The hydrogen bond in water is a dynamic attraction between neighboring water molecules involving one hydrogen atom located between the two oxygen atoms.
Explanation:
Traditional forms shows the evolutionary steps between species
Answer:
4. According to what is observed in the diagram, the maltose (substrate) binds to the maltase (enzyme) to obtain glucose molecules (product), in a process of <u>hydrolysis</u> of the maltose.
5. Three factors that can affect intestinal maltose activity - slowing it down or stopping it - are temperature, pH and substrate depletion.
Explanation:
4. Enzymes, such as maltase, have the function of making a reaction faster and decreasing the activation energy. <u>Maltase is responsible for breaking down a maltose molecule, a dimer, into two glucose monomers</u>, which is a hydrolysis reaction of the bonds that hold glucose molecules together.
5. There are several factors that can cause the decrease or cessation of the activity of an enzyme. <u>Enzymes are activated when substrate is available and work best under ideal temperature and pH conditions</u>. When there are alterations of these factors, the enzyme will reduce or stop the reaction in which it intervenes.
- <em><u>pH</u></em><em>: when the pH increases or decreases it produces a decrease in the speed of reaction that catalyzes an enzyme. Very high or low pH levels can denature the enzyme and make the expected reaction not occur.
</em>
- <em><u>Temperature</u></em><em>: like pH, changes in temperature can slow or stop maltase activity.
</em>
- <em><u>Substrate availability</u></em><em>: It is a fact that when the specific substrate of an enzyme becomes depleted, the rate of reaction slows down, stopping when no substrate is available.</em>
Answer:
I think it is <em>true</em>
<em>hope</em><em> it</em><em> </em><em>helps</em>
