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