The α and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin. Why might this be the case? Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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The a and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are
hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin.
Why might this be the case?
O Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other
myoglobin molecules.
O Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through
van der Waals interactions.
Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms
globular structures.
Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.
Transcribed Image Text:The a and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin. Why might this be the case? O Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. O Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.
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