Assessing the dissociation behavior of aspartate residues in a membrane
As described in the text, the pKa values of Asp85 and Asp96 of bacteriorhodopsin are shifted to high values (more than 11) because of the hydrophobic environment surrounding these residues. Why is this so? What would you expect the dissociation behavior of aspartate carboxyl groups to be in a hydrophobic environment?
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