30 Questions
Which molecule carries CO2 from the tissues to the lungs?
Hemoglobin
In terms of structure, what is unique about hemoglobin compared to myoglobin?
It has a quaternary structure
What is formed spontaneously and by the RBC enzyme carbonic anhydrase?
HCO3-
Where does CO2 originate in the process of respiration?
Tissues
Which molecule has the capacity to transport 14% of CO2 and H+ in the blood?
Hemoglobin
What features of hemoglobin give it unique 'allosteric effects'?
Quaternary structure
Which enzyme is responsible for the formation of HCO3- during respiration?
Carbonic anhydrase
What is the molecule released when CO2 is exhaled in the lungs?
H2O
What does high [O2] in the lungs favor in terms of hemoglobin?
Oxygenated Hb
Which protein has only tertiary structure and lacks quaternary structure?
Myoglobin
What is the primary driving force for the formation of globular protein structure?
Hydrophobic interactions between amino acids
Which level of protein structure is most responsible for the overall shape of a globular protein?
Tertiary structure
What is the primary function of the prosthetic group in hemoglobin and myoglobin?
To facilitate oxygen binding
How do hemoglobin and myoglobin differ in terms of their quaternary structure?
Hemoglobin has a tetrameric structure, while myoglobin is monomeric
What is the role of molecular cooperativity in hemoglobin?
To enhance oxygen binding affinity
What is the primary difference between the functions of hemoglobin and myoglobin?
Hemoglobin transports oxygen from the lungs to the tissues, while myoglobin stores oxygen in the muscles
What is the significance of the hierarchy of protein structure in understanding globular proteins?
It enables the understanding of protein structure-function relationships
How do hydrophobic interactions contribute to the stability of globular proteins?
By minimizing the exposure of hydrophobic residues to water
What is the primary characteristic of water-soluble globular proteins?
They have a low proportion of hydrophobic residues
What is the role of allosteric effects in hemoglobin?
To regulate oxygen binding affinity
Explain the role of carbonic anhydrase in the transport of CO2 in the blood.
Carbonic anhydrase catalyzes the formation of HCO3- from CO2 which is crucial in transporting CO2 in the blood.
How does a high concentration of O2 in the lungs affect hemoglobin?
High [O2] in the lungs favors oxygenated hemoglobin.
What is the primary function of myoglobin?
Myoglobin functions to store oxygen in muscle cells.
Differentiate between hemoglobin and myoglobin in terms of quaternary structure.
Hemoglobin has quaternary structure while myoglobin does not.
How does the formation of HCO3- by carbonic anhydrase in red blood cells impact pH levels?
Formation of HCO3- by carbonic anhydrase reduces pH, promoting further O2 dissociation.
What is the primary difference between hemoglobin and myoglobin?
Hemoglobin has quaternary structure while myoglobin does not.
Explain the significance of allosteric effects in hemoglobin.
Unique allosteric effects in hemoglobin impact its function and oxygen affinity.
How are CO2 and H+ transported from tissues to the lungs in the blood?
Only 14% of CO2 and H+ are transported bound to hemoglobin, while the rest is transported as HCO3-.
Briefly explain the formation of HCO3- during respiration.
CO2 combines with water to form bicarbonate ion and hydrogen ion.
Compare the tertiary structures of hemoglobin and myoglobin.
Hemoglobin and myoglobin have very similar tertiary structures.
Explore the characteristics and functions of structural proteins such as actin and tubulin which polymerize into long fibers, as well as the oxygen-carrying globular proteins myoglobin and hemoglobin. Learn about the heme group, tertiary structures, and biological roles of these proteins.
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