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

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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

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3
Q

Four functions of myoglobin

A
  1. Acts as a local reserve of O2 during intense exercise
  2. Store O2 in aquatic animals
  3. Facilitates O2 diffusion through muscle tissue
  4. Inactivates NO and scavenging reactive O2 species
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4
Q

Where are hemoglobin and myoglobin found in the body?

A

Hemoglobin: RBC cells (transporter)
Myoglobin: Striated muscles (receiver)

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5
Q

Define

Ligand

A

ions or neutral molecules that bond to a central metal atom or ion

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6
Q

The greater affinity of X for Y the ____ XY we will have at any [] of Y or X

A

more

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