title: Pressure stability of proteins at their isoelectric points.
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.
authors.affiliation: Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA.
authors.forename: Gene
authors.initials: G
authors.lastname: Kidman
authors.forename: Hyun
authors.initials: H
authors.lastname: Park
authors.forename: Dexter B
authors.initials: DB
authors.lastname: Northrop
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006874:Hydrostatic Pressure; D007526:Isoelectric Point; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D015003:Yeasts / Q000201:enzymology
chemical_list: D011506:Proteins; D000426:Alcohol Dehydrogenase