Normal hemoglobin is a tetramer, consisting of two molecules of β-globin and two molecules of α-globin; normal hemoglobin molecules do not associate with each other. in sickle-cell disease, the change in a single amino acid results in mutant hemoglobin tetramers, which associate with each other and assemble into large fibers. based on this information alone, what can we conclude about the changes in the structure of sickle cell hemoglobin as compared to normal hemoglobin?

Established on the data, sickle cell hemoglobin displays altered primary structure and altered quaternary structure; the secondary and tertiary structures may or may not be altered. The sickle cell disease is a cluster of disorders that disturbs hemoglobin, the molecule in red blood cells that transports oxygen to cells all over the body. A person with this disorder have uncharacteristic hemoglobin molecules named hemoglobin S which can interfere with red blood cells into a sickle or crescent shape.

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