Hemoglobin has quaternary structure: a. true b. false 2. individual alpha-helices found in hemoglobin are stabilized by ionic bonds: a. true b. false 3. hemoglobin would be synthesized by a ribosome on the rough er: a. true b. false 4. a dna mutation that affects the primary structure of the alpha-globin protein subunit would also affect the primary structure of the beta-globin protein subunit. a. true b. false

Further Explanation:

A polypeptide chain leads to formation of proteins. There are exceptions to proteins; some of them are formed by the association of more than one polypeptide chain (sub-units). These proteins are termed to be as Quaternary proteins.  

Depending upon the number of protein chain subunits proteins can be of following types;

Hemoglobin is one such quaternary protein which is formed by as of polypeptide chains association. The polypeptide chains found in hemoglobin are;

The 3D structure of the molecule is as the result of the hydrogen bond interactions. This interactions gives the molecule it characteristic shape and helps it to carry out it functions effectively.

Formation of hemoglobin occurs differently depending on the components. The hemoglobin molecule has two components that are heme and globin.

The Heme part is formed at following location;

While, the ‘globin’ part is synthesized by the ribosomes, in the cytosol of the cell. The change or mutation in one of the chain won’t affect the other chain but surely the overall functions and physicality will be altered. For example, the replacement of glutamic acid codon (GAG) to a valine codon (GTG) can lead to sickle cell anemia.

Learn more:

1. Learn more about cell organelle

2. Learn more about the diffusion

3. Learn more about the plant

Answer Details:

Grade: High School

Subject: Biology

Topic: Hemoglobin

Keywords:

Hemoglobin, quaternary structure, rough ER, myoglobin, structure, globin, folding, hydrogen bond, heme, variant, oxygen, erythrocytes, beta, alpha.

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