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BCH 100 Lecture 7: Myoglobin and Hemoglobin

front 1

How does oxygen alter the Heme and Globin Structure?

back 1

The oxygen pulls the Fe group down, thus aligning the entire molecule

front 2

What is the T state?

back 2

The tense state of Hemoglobin. The affinity for oxygen goes down, the affinity for CO2, H+, and 2,3-BPG binding goes up. There is a larger central cavity within the globin

front 3

What is the R state?

back 3

The relaxed state of Hemoglobin. The affinity for oxygen goes up, the affinity for H+, CO2, and 2, 3- BPG binding goes down. Has a smaller central cavity

front 4

Describe the journey of these Hemoglobins in the body.

back 4

The lungs inhale oxygen which are picked up by R state hemoglobins and carried through the arteries throughout the body distributing oxygen into muscles and tissues. Once it releases the oxygen, it goes into T state and picks up CO2 which is carried through the veins back into the lungs to be exhaled out into the environment again.

front 5

What is Fetal Hemoglobin?

back 5

Its the hemoglobin found active in a fetus' blood. Fetal hemoglobin has a much higher affinity for oxygen than an adult's hemoglobin due to the need to grow and develop more. This leads to pregnant mothers being more prone to breathlessness because more of the oxygen they breathe in if going to the fetus.

front 6

What is Sickle Cell Disease?

back 6

It is a genetic disease that cause hemoglobins to take a more sickle/ moon like shape. It increases chances of blood not traveling properly throughout the body from blockages and clogs due to its odd shape. A Glutamate replaced by a Valine. However, those who are heterozygous for this gene show resistance to Malaria

front 7

Explain the curves on a BPG graph

back 7

A right shift has a lower affinity for oxygen. They unload easier but find it hard to load an oxygen. A left shift has a lower affinity for oxygen. They find it hard to unload but quite easy to load the oxygen to them.