BIOCH200 Lecture Notes - Myoglobin, Hemoglobin, Histidine

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**note: the pocket in myoglobin that is available for heme group bonding is. *kd dissociation constant the [l] ( l = ligand) needed for 50% saturation to be achieved. ( subunits are. All three consist of 8 -helices: oxygen binding sites are invariant (is the same as in the other polypeptides) Bind to the same helix of the polypeptide and the same histidine molecules. *conservative substitution: *amino acid substitution causes minimal protein property and conformational changes, *amino acid change must be within the same group and have the same properties. *critical substitution: *amino acid substitution that results in large conformation changes and therefore change/loss of protein function. Aspartate (negatively charged) being replaced with phenylalanine (a very hydrophobic amino acid: hyperbolic vs. sigmoidal curve relationships in ____-globin, *hyperbolic affinity remains constant. Myoglobin: *sigmoidal affinity changes based on how many ligands are already bound to the protein (cooperative binding) *as more oxygen molecules bind to hemoglobin, its affinity for oxygen decreases.

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