00:01
Hello everyone, in this question we have the case of a mutant hemoglobin and that is hemoglobin ohio group.
00:09
The normal hemoglobin is represented in this question as hb a molecule.
00:15
In this case, what is happening is that in case of hemoglobin ohio, there is a particular mutation in the beta chain at 142 position.
00:24
This alenine amino acid is being replaced or mutated to an aspartic acid residue.
00:31
This is, alenine, okay, that aline was a neutral or there was basically no charge because aline does not have any charge, but this aspartake, as it is negatively charged.
00:44
So there is an introduction of negative charge due to this particular mutation.
00:50
What happens due to this negative charge is that it will destabilize the one of the most important iron bridge that we require or that is required by hemoglobin to maintain its stability.
01:02
Of the t state.
01:03
So it basically destabilizes a particular ion group and that iron pair in this case is beta 146 histidine that is hiss and beta 94 spartic acid residue.
01:19
When this pair it gets disturbed.
01:22
So what happens is it will lead to the destabilization of this t state.
01:27
Hemoglobin it has two states, r in t state, and this t state, its stability decreases...