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Updated: Jul 11, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Pressure stability of proteins at their isoelectric points
Gene Kidman1, Hyun Park, Dexter B Northrop
1Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA.
Abstract:
Yeast alcohol dehydrogenase is slowly denatured at moderate hydrostatic pressure (t(1/2) approximately equals 30 min at 2 kbar and pH 7). The extent of denaturation is pH dependent with maximal stability near the isoelectric point of the protein, pH = 5.4. While not a surprising finding, it appears that this phenomenon has not been documented before (or at least not identified) despite many investigations into the pressure stability of proteins. Consideration of changes in the net charge of proteins far from their isoelectric points may explain other pressure effects as well.
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