Send the link below via email or IMCopy
Present to your audienceStart remote presentation
- Invited audience members will follow you as you navigate and present
- People invited to a presentation do not need a Prezi account
- This link expires 10 minutes after you close the presentation
- A maximum of 30 users can follow your presentation
- Learn more about this feature in our knowledge base article
Do you really want to delete this prezi?
Neither you, nor the coeditors you shared it with will be able to recover it again.
Make your likes visible on Facebook?
You can change this under Settings & Account at any time.
Transcript of Alpha subunit
Deoxygenated VS. Oxygenated Hemoglobin
Hemoglobin has four sub-units as seen pictured above: two alpha units and two beta units. When hemoglobin becomes deoxygenated after flowing through the blood stream, the four subunits enter a T-State or tense state.(Hudon-Miller, 2012) The Iron Atoms of each sub-unit flexes the Heme group into a triangle like position, that pulls the Iron Atom up into each subunit. The tense state makes it more difficult for oxygen molecule to adhere to each Iron Atom. But once the hemoglobin reach the lungs and one oxygen molecule attaches to one of the four Iron Atoms, the other three heme group inside of the sub-units change shape. The heme groups relaxes allowing the other three Iron atoms to pickup oxygen with ease. This relaxed state is known at the R-State. The process were the molecule changes shape to making it easier for the oxygen to attach to the molecule is called Cooperativity. Once oxygenated the hemoglobin turns from a blue color to a bright right red color. (Hudon-Miller, 2012)
Veronica Weissner Task 208.5.3-01-05 Protein Function
The polymer strands that are formed because of the mutation of the sickle cell make the uptake of oxygen much harder than that of the normal red blood cell. The sickle shape causes the cell to stick together when they are de-oxygenated. The de-oxygenated cells get caught in the blood vessels making them unable to return to the lungs to uptake oxygen. They stuck cells cause pain as the CO2 builds up in the tissue. When sickle cells make it back to the lungs, oxygen helps to break up the strands that were formed when the cells lost there oxygen molecule. (Hudon-Miller. 2012)
When the sickled cells stick together they can get caught in the veins/arteries causing hypoxia to surrounding tissue. This is know as sickle cell crisis and a great deal of pain can come to those who suffer from Sickle Cell Disease.
Normal red blood cells are round in shape with a concave centers containing one hydrophobic pocket on each surface. Normal Red blood cells live approximately 120 days, floating freely with ease, flexing throughout the body, even into the smallest blood vessels, caring oxygen to tissue and remove toxic molecule carbon dioxide.(Sanders. 2014)
Normal Red Blood cell
Sickle cells have a crescent shape because the sixth protein on the Beta subunit has a defect. The sixth protein has a non-polar, non-charged, hydrophobic protein called Valine, instead of the polar and negative charged Glutamic Acid. (Hudon-Miller 2012) The mutation turns the water loving molecule into a hydrophobic molecule. The hydrophobic valine sticks itself into the hydrophobic pocket of other sickle cells causing polymers that form fibers during de-oxygenation state. This mutation of the Sickle cell causes it to become stiff and inflexible unlike normal red blood cells.(Sanders.2014) The change in shape makes the sickle cell hard to pickup and carry oxygen causing people who suffer from sickle cell disease to enter a crisis state. (Sanders. 2014)
CO2 is produced by all cells during a metabolic process called the citric acid cycle. Hemoglobin travels through the blood stream carry oxygen from the lungs to the tissue through out the body. As the hemoglobin travels through the blood stream it releases oxygen in exchange for CO2 molecules released by cells. The more CO2 present decreases the pH level and the less Co2 present increases the pH level. The blood's normal pH ranges from 7.2 to 7.4. Tissue that is closer to the lungs usually has a higher pH level around 7.4. The tissue in the extremities has a lower more acid pH around 7.2. Bohr Effect is the hemoglobin's ability to hold on to the oxygen molecules depending on the pH level in the blood. The higher the pH level is in the blood the more tightly the hemoglobin holds on to the oxygen molecules. The more acidic the pH level is in the blood the more quickly the hemoglobin is going to release the oxygen. (Hudon-Miller. 2012)
Sickle cell cross section
Above is two parents who have the sickle cell trait gene, along with a normal hemoglobin gene. When a child is created the child can receives one gene from each parent. Leaving the child with 25% chance of not requiring the gene at all. 50% change of having the sickle cell trait and 25% chance of having sickle cell disease. (Hudon-Miller. 2012)