Function of the hemoglobin protein

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How would the mutations below modify or alter the function of the hemoglobin protein? Provide in-text citations and scholarly references in 7th edition apa format. Utilize 200 words or more: The most common characterized hemoglobin variant are the unstable ones (Thom, et al., 2013). These Hb variants typically have an amino acid deletion, elongation, and/or substitution. These are most detrimental in both the heme pocket and the hydrophobic regions of the domain where it will then both affect the oxygen binding. Worst case scenarios, there will be significant precipitation and aggregation. One main issue they list are substitutions with proline, which then affect the main alpha helix structures. On the opposite side of the spectrum, high oxygen affinity variants are dangerous as well. Even though it seems better, without being able to release the oxygen to the cells and the body, the Hb is also preventing oxygen from going to their destinations. This is typically because the alpha1beta2 is altered through substitutions, since they are the main interface for the T to R state for oxygen binding. These changes then shift equilibrium to favor the oxygenated R form and prevent the usual normal release of oxygen.

Reference no: EM133822064

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