Function of Hemoglobin

The diagram shows a haemoglobin molecule. Which identifies the different parts of the molecule?

• 1: alpha helix, 2: beta pleated sheet, 3: binding site, 4: hydrophobic amino acids
  
• 1: hydrophobic amino acids, 2: beta pleated sheet, 3: prosthetic group, 4: binding site
• 1: prosthetic group, 2: hydrophobic amino acids, 3: alpha helix , 4: hydrophilic amino acids
• 1: prosthetic group, 2: hydrophilic amino acids, 3: alpha helix , 4: hydrophobic amino acids

The ion found in the haem group is what

• Mg²⁺

• O^2-

• Fe²⁺

• Fe³⁺

Which of the following is NOT the structure of haemoglobin?

• Each haemoglobin molecule contains 4 haem groups

• Haemoglobin has a quaternary structure

• Each haem group in haemoglobin can bind with 4 molecules of oxygen

• Each haemoglobin molecule has 2 α-chain and 2 β-chain polypeptide subunits

The main blood vessel responsible for taking oxygenated blood to the body is the

• pulmonary artery

• aorta

• vena cava

• pulmonary veins

What is the name of the molecule formed when oxygen binds to haemoglobin?

• oxyhaemoglobin

• oxygen-haemoglobin

• carbaminohaemlobin

• oxyglobin

Carbon dioxide and water combine to form

• hydrogen carbonate ions

• hydrogen ions

• carbonic acid

• hydrogen bicarbonate

Oxyhaemoglobin gives up O₂ when …

• CO₂ partial pressures are high

• Body temperature is lowered

• pH values are high

• O₂ partial pressure are high

Tags

NGSS.HS-LS1-3

The Bohr Effect/Shift moves the oxygen saturation curve in what direction

• up and left

• down and right

• down and left

• up and right

At the highest partial pressures of oxygen, the saturation of oxygen slows down because

• the haemoglobin becomes saturated

• the haemoglobin becomes denatured

• the haemoglobin is too cold

• the oxygen is displaced by carbon dioxide

which of the following explains the meaning of the Bohr effect?

• The effect of the partial pressure of oxygen in blood on the affinity of haemoglobin towards carbon dioxide.

• The effect of the partial pressure of carbon dioxide on the dissociation of oxyhaemoglobin.

• The affinity of haemoglobin toward oxygen.

• The affinity of haemoglobin towards carbon dioxide.