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29.09.2019 •
Biology
Select the false statement below about the structure of myoglobin.
a. the o2-binding pocket of myoglobin contains several nonpolar amino acid sidechains that can interact favorably with a nonpolar molecule of o2.
b. the polypeptide of myoglobin provides a pocket for o2 to fit, and stabilizes the bound o2 via hydrogen bonding with the distal his.
c. the polypeptide of myoglobin protects the heme iron from oxidation.
d. the 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.
e. myoglobin has a single polypeptide chain so it has 1o, 2o, 3o and 4o structure.
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Ответ:
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.
Ответ:
Crossing-over is the exchange of genetic material between homologous chromosomes. It results in new combinations of genes on each chromosome. When cells divide during meiosis, homologous chromosomes are randomly distributed to daughter cells, and different chromosomes segregate independently of each other.
Explanation:
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