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Pressure Stability of Proteins at their Isoelectric Points

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Yeast alcohol dehydrogenase is slowly denatured at moderate hydrostatic pressure (t1 / 2 ? 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.

Keywords: Isoelectric point; barostability; cytochrome c; hydrostatic pressure; myoglobin; protein denaturation; protein folding; thermostability; volume of ionization; yeast alcohol dehydrogenase

Document Type: Review Article


Affiliations: Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, U.S.A.

Publication date: 2004-12-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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