From the videos, I learned that two different types of behavior exhibited by

myoglobin and hemoglobin are related to the functions of these proteins. Hemoglobin differs
from myoglobin in containing polypeptide subunits instead of one. Interactions between
multiple polypeptide subunits of a protein are called quaternary structure. Myoglobin has the
function of oxygen storage in muscle great. Structural changes during binding of small
molecules are characteristic of allosteric proteins such as hemoglobin. Hemoglobin has
different quaternary structures in the bound (oxygenated) and unbound (deoxygenated)
forms. The two b-chains are much closer to each other in oxygenated hemoglobin than in
deoxygenated hemoglobin. The change is so marked that the two forms of hemoglobin have
different crystal structures.

In protein purification, steps typically include busting cell open, centrifuging cellular
components apart from the cytoplasm, and using techniques that separate molecules by
several different processes. Thus, most protein requires more than one method to be purified.
Techniques for protein purification often rely on the structural components of proteins.
Isolation of protein from cells requires breaking open the cells, centrifugation to remove
insoluble debris, and the application of protein isolation techniques to purify desired proteins
from the soluble fraction of the cells. Moreover, proteins can have negative, positive or no
charge at all. To be separated in electrophoresis, they must be converted from folded entities
into rods with uniform negative charge.