Ionic strength-dependent structural transition of proteins at electrode surfaces
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19294262
DOI
10.1039/b822274f
Knihovny.cz E-resources
- MeSH
- Electrodes * MeSH
- Phosphates chemistry MeSH
- Hydrogen-Ion Concentration MeSH
- Osmolar Concentration * MeSH
- Potentiometry MeSH
- Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Phosphates MeSH
- Proteins MeSH
- sodium phosphate MeSH Browser
Using constant current chronopotentiometry we showed that in 50 mM sodium phosphate (pH 7) bovine serum albumin and some other proteins were not significantly denatured at a bare mercury electrode while at higher phosphate concentrations they underwent electric field-driven denaturation on the electrode surface.
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