The answer is bohr hope this helps :)
<h3><u>Answer;</u></h3>
The statements that are True are;
- Upon binding a molecule of oxygen, Hb undergoes a conformational change that makes the binding of subsequent O2 molecules easier.
- The conformational change induced in Hb upon binding oxygen is the result of a small movement (0.2 Å) of the iron cation in the center of heme.
- Site-directed mutagenesis studies have indicated that the cooperativity of O2 binding in Hb is attributable to the movement of the F helix in Hb.
<h3><u>Explanation</u>;</h3>
- Hemoglobin is a key pigment in the blood that transports oxygen gas to all the tissues in the body. It is made up of two types of chains; that is two alpha chains and two beta chains.
- in its deoxygenated state hemoglobin has a low affinity for oxygen compared to myoglobin. When oxygen is bound to the first subunit of hemoglobin it leads to subtle changes to the quaternary structure of the protein. This in turn makes it easier for a subsequent molecule of oxygen to bind to the next subunit.
Answer:
The molecular structure affects solubility mainly biased on its polarity or bonded ions.
Explanation:
Polar molecules will better interact with the water molecules and will dissolve easier. Nonpolar molecules can dissolve if they are small enough, however they don't interact well with the polar molecules. Bonded ions, such as NaCl split into a cation Na and an anion Cl which the positive charge on the Na will be attracted to the oxygen, and the negatively charged Cl will be attracted to the positive Hydrogen.
**Remember this rule, like dissolves like, meaning nonpolar dissolves nonpolar and polar dissolves polar.
I hope this helps!
