Aquaporin Membrane Molecules Lab Report

1a. Aquaporins are membrane proteins that have fourteen various structures however the most common form is that of a homotetramer. The homotetramer is often found in the membrane and composed of four aquaporin membranes. The structural arrangement creates a fifth channel in the middle that allows for gas transportation.

1b. The direction of H2O molecular flow through a channel is determined by an osmotic gradient.

1c. One of the mechanisms that prevents proton channeling is due to the (ar/R) and NPA regions. The mechanism occurs based on the arrangement of the water bi-directional water chains. This arrangement causes the hydrogens to be pointed away from the inner channel. This indicates that the hydrogen bonds are broken and the dipole moment is disrupted.

2. One of the mechanisms used is gating. Gating is when water transport is controlled through conformational changes at the protein level. The other mechanisms used to control aquaporin water transport is through changing the density of the aquaporin at a specific membrane. The second mechanism listed involves trafficking in which proteins are alternated between target
Magnesium Sulfate works by increasing the osmotic pressure in the intestinal tract to induce diarrhea and by increasing fecal water content. AQP3 transport water from a low osmotic pressure on the luminal side of the membrane to a high osmotic pressure on the vascular side of the membrane under normal physiological conditions within the colon. When magnesium sulfate is taken the reverse happens, it goes from the vascular to the luminal side, an area of high pressure to low pressure, as a result of increased osmotic pressure in the colon and diarrhea occurs. After 2 hours it is noted that water was not transported because AQP3 expression levels were not high enough. Over time though such as five hours, the levels begins\ to increase thus moving large amounts of water from the vascular side to the luminal side resulting in