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Why does a hydrophobic environment increase the pKa of Histidine?
Wiki User
∙ 14y ago
The pKa, or acid dissociation constant, of an amino acid is strongly tied to the properties of the surrounding solvent. The hydrophobic core of a protein is a distinctly different environment than the water exposed surface of the protein and the pKa in the core is different than the normal, solvent exposed pKa. This is related to the dielectric constant, or the ease at which charge is "felt" over a distance, which is much lower in the hydrophobic core of the protein. In addition, the now fixed locations of other possibly charged amino acids nearby will also impact the pKa of the residue.
Wiki User
∙ 14y ago
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Why histidine is often found at the active-site of enzyme?
it has pKa of 6.8
Why histidine present frequently in an active site of enzyme?
The imidazole side chains and the relatively neutral pKa of histidine (ca 6.0) mean that relatively small shifts in cellular pH will change its charge. For this reason, this amino acid side chain finds its way into considerable use as a coordinating ligand in metalloproteins, and also as a catalytic site in certain enzymes
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