Chem Task 3 - Protein Function

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Task 3 - Protein Function When oxygen binds to hemoglobin Hemoglobin is what we call a quaternary structure, and inside this structure are a few components that help it carry oxygen. The “heme” is a structure that lies within the protein coils of the hemoglobin. Iron attaches itself to the heme, and when the hemoglobin enters the lungs, oxygen attaches to the iron on the heme. The hemoglobin has two states, and when we are discussing the attaching of oxygen, we are talking about the “relaxed” state of hemoglobin. When you have relaxed hemoglobin, you’ll usually have a higher Ph, along with a lower CO2. This state favors the oxygen attaching to the hemoglobin. Once the oxygen attached, the hemoglobin will become tense, and the entire structure will undergo a sligh change in shape. The color of the hemog;obin will also become a ruby or brilliant red. When Hemoglobin releases oxygen As the hemoglobin travels, it will encounter places when the Ph is lower, and the CO2 is higher. These states will cause the hemoglobin to release some of its oxygen to the surrounding tissues. The structure will again relax as it releases the oxygen from its iron. once this happens, the color becomes a dull red, or possibly blueish, depending on the individual and any cardiopulmonary conditions they might have. Differences • Structure is tense (releasing O20 or relaxed (accepting O2). • Color is bright red (oxygenated) or dark red to blueish (non-oxygenated). • High Ph and low CO2 = O2 attachment, Low Ph and high CO2 = O2 release The Bohr Effect Hemoglobin vs Myoglobin Structure Hemoglobin vs Myoglobin Structure Molecular Difference between Normal and Sickle forms of Hemoglobin. The Difference between Normal and Sickle RBCs Compare how diseased cells differ from normal red blood cells in their capacity to transport and deliver oxygen.
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