Select the FALSE statement below about the structure of myoglobin.

AThe O2-binding pocket of myoglobin contains several nonpolar amino acid sidechains that can interact favorably with a nonpolar molecule of O2.

BThe polypeptide of myoglobin provides a pocket for O2 to fit, and stabilizes the bound O2 via hydrogen bonding with the distal His.

CThe polypeptide of myoglobin protects the heme iron from oxidation.

DThe active site of deoxy myoglobin is 5-coordinate with a histidine occupying one axial position while the other axial position is left open for oxygen binding.

EMyoglobin has a single polypeptide chain so it has 1o, 2o, 3o and 4o structure.

Question

ziR0moutriffetdado ziR0moutriffetdado

21-11-2016
Biology

Answered

Select the FALSE statement below about the structure of myoglobin.

AThe O2-binding pocket of myoglobin contains several nonpolar amino acid sidechains that can interact favorably with a nonpolar molecule of O2.

BThe polypeptide of myoglobin provides a pocket for O2 to fit, and stabilizes the bound O2 via hydrogen bonding with the distal His.

CThe polypeptide of myoglobin protects the heme iron from oxidation.

DThe active site of deoxy myoglobin is 5-coordinate with a histidine occupying one axial position while the other axial position is left open for oxygen binding.

EMyoglobin has a single polypeptide chain so it has 1o, 2o, 3o and 4o structure.

Verified Answer :

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JcAlmighty JcAlmighty · Answer 1 · 2016-11-21T12:31:48-05:00

The answer is e. Myoglobin has a single polypeptide chain so it has 1o, 2o, 3o and 4o structure.

Myoglobin is an iron and an oxygen binding protein. It has a single polypeptide chain. Proteins with the single polypeptide chain cannot have quaternary (4o) structure. 4o structure of proteins includes an arrangement of multiple folded polypeptide chains (subunits) in a multi-subunit complex. Therefore myoglobin cannot have 4o structure as the single chain polypeptide. All other choices are correct.