BIOMOLECULES AND ENZYMES

BIOLOGY

PROTEINS

Question [CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
Haemoglobin, a globular protein, consists of four polypeptide chains, two alpha chains and two beta chains. In normal individuals, in the DNA which codes for each beta chain, the sixth triplet has a code for glutamic acid. In individuals with sickle cell anaemia this base triplet mutates and codes for valine. What does this mutation change in the haemoglobin molecule?
A
A the iron content
B
B the primary structure
C
C the quaternary structure
D
D the secondary structure
Explanation: 

Detailed explanation-1: -The specific base sequence for these amino acids is: GTG/CAC/CTG/ACT/CCT/GAG. Sickle cell hemoglobin (Hemoglobin S) results when, glutamic acid that is normally present in the sixth position on the beta globin chain is substituted with valine.

Detailed explanation-2: -A hemoglobin molecule is made up of four polypeptide chains, two alpha chains of 141 amino acid residues each and two beta chains of 146 amino acid residues each.

Detailed explanation-3: -Hemoglobin is an example of a globular protein. It consists of four polypeptide chains, each folded onto itself. Each chain is attached to a heme group–a ring-like structure with an iron atom at the center. It is at these iron atoms that oxygen molecules bind to hemoglobin.

Detailed explanation-4: -The hemoglobin molecule is made up of four polypeptide chains (Alpha 1, Beta 1, Alpha 2, Beta 2), noncovalently bound to each other. There are four heme-iron complexes. Each chain holds a heme group containing one Fe++ atom. The heme-iron complexes are colored red because they give hemoglobin its red color.

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