What is the difference between normal hemoglobin and the hemoglobin associated with sickle-cell

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What is the difference between normal hemoglobin and the...

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Key Concepts

Point Mutation in Beta-Globin Chain

A single nucleotide mutation in the gene coding for the beta chain of hemoglobin results in the substitution of a hydrophilic glutamic acid with a hydrophobic valine at the sixth position. This small change in the amino acid sequence is the molecular cause of sickle-cell hemoglobin and is a classic example of how a point mutation can have considerable effects on protein function.

Altered Hemoglobin Structure and Interaction

The substitution of a hydrophilic amino acid with a hydrophobic one in sickle-cell hemoglobin changes the overall surface properties of the protein. This alteration encourages abnormal interactions between hemoglobin molecules, leading them to stick together under low oxygen conditions, unlike the normal hemoglobin which remains soluble and disperses evenly.

Impact on Solubility and Polymerization

Due to the presence of the hydrophobic valine, sickle-cell hemoglobin becomes less soluble in the deoxygenated state. This reduced solubility leads to the polymerization of hemoglobin molecules, forming long fibers that deform the red blood cells into a characteristic sickle shape, ultimately contributing to the clinical manifestations of the disease.

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