00:02
Okay, so for 3a, hemoglobin has four tertiary structure protein chains, which enable them to perform the function of transportation of o2 around the body.
00:12
So the different levels of polypeptide structures are the primary structure, which is just the string of amino acid secondary structure, which are not remaining in a three line.
00:22
They're in a 3d structure.
00:23
Tertiary structure, which is the final form and quaternary form, which is complex.
00:27
So hemoglobin is complex or quaternary.
00:36
Give it a fancy name here.
00:44
So it's all alpha helices, and each alpha helis has a secondary polypeptide structure made of amino acids.
00:50
The sequence of amino acids in turn are a primary structure of hemoglobin.
00:55
The four secondary structural chains are, or alpha helices surround the iron molecule, which is called the heem group.
01:02
The oxygen binds to the heen group, and there are four hemisites for the oxygen binding in hemoglobin.
01:08
Structural changes occur as oxygen binds to it.
01:10
First, oxygen binds to difficult, but the other three oxygen molecules bind easily...
