Pressure Stability of Proteins at their Isoelectric Points

Title: Pressure Stability of Proteins at their Isoelectric Points

Volume: 11 Issue: 6

Author(s): Gene Kidman, Hyun Park and Dexter B. Northrop

Affiliation:

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

Abstract: 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.

Cite this article as:

Kidman Gene, Park Hyun and Northrop B. Dexter, Pressure Stability of Proteins at their Isoelectric Points, Protein & Peptide Letters 2004; 11 (6) . https://dx.doi.org/10.2174/0929866043406157

DOI https://dx.doi.org/10.2174/0929866043406157	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305