C7: Structure of Haemoglobin Flashcards
Students can describe structure of Haemoglobin and how it is adapted to carry oxygen.
P1: What kind of protein is hemoglobin, and how is it put together?
Haemoglobin is a conjugated protein with quaternary structure.
P2: How many α-polypeptides and β-polypeptides make up a hemoglobin molecule, and how do they arrange to form the protein’s structure?
It consists of 2 α-polypeptides and 2 β-polypeptides subunits that coiled to form a globular protein.
P3: What does each part of hemoglobin carry?
Each polypeptide subunit contains a prosthetic group, haem.
P4: What’s in the center of the hemoglobin parts, and what does it do with oxygen?
Haem/ Ferum atom in the centre can binds with one oxygen molecule.
P5: How many oxygen molecules can one hemoglobin molecule bind?
One haemoglobin molecule can bind with four oxygen molecules.
P6: What happens to the other haem groups when one oxygen molecule binds to a haem group in hemoglobin?
When one oxygen molecule binds to one haem group, it causes conformational changes to the other haem groups.
P7: Why is it easier for hemoglobin to pick up more oxygen once it has some?
The second oxygen binds more easily followed by the third and fourth oxygen molecules // Haemoglobin shows cooperativity.
P8: What happens when oxygen binds to hemoglobin, and what is the role of oxyhemoglobin in the body’s oxygen transport system?
When oxygen binds with haemoglobin, oxyhaemoglobin is formed and carried to the body tissues to supply oxygen to the tissues.
