title: Ionic strength-dependent structural transition of proteins at electrode surfaces.
abstract: 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.
authors.affiliation: Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Královopolská 135, 612 65, Brno, Czech Republic. palecek@ibp.cz
authors.forename: Emil
authors.initials: E
authors.lastname: Palecek
authors.forename: Veronika
authors.initials: V
authors.lastname: Ostatná
mesh_terms: D004566:Electrodes; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010710:Phosphates / Q000737:chemistry; D011199:Potentiometry; D011506:Proteins / Q000737:chemistry*
chemical_list: D010710:Phosphates; D011506:Proteins; C018279:sodium phosphate