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Chem Task 3 - Protein Function Essay

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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.

• 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

A Red Blood Cell RBC is a concave, disk-shaped cell that is loaded with Hemoglobin Hb that...

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