Protein Function Flashcards
1
Q
How are myoglobin and hemoglobin different in their structures?
A
Myoglobin:
* Mononmer
* 1 polypeptide chain (154 aa and 1 domain)
* Only a tertiary structure
Hemoglobin:
* Oligomer
* 4 polypeptide chains (each has 1 domain)
* has quaternary structure
2
Q
What do red blood cells do in capillaries?
A
Hemoglobin (a protein within RBCs) binds to O2 in the lungs and releases it in the tissues
3
Q
Four functions of myoglobin
A
- Acts as a local reserve of O2 during intense exercise
- Store O2 in aquatic animals
- Facilitates O2 diffusion through muscle tissue
- Inactivates NO and scavenging reactive O2 species
4
Q
Where are hemoglobin and myoglobin found in the body?
A
Hemoglobin: RBC cells (transporter)
Myoglobin: Striated muscles (receiver)
5
Q
Define
Ligand
A
ions or neutral molecules that bond to a central metal atom or ion
6
Q
The greater affinity of X for Y the ____ XY we will have at any [] of Y or X
A
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