Ionic strength-dependent structural transition of proteins at electrode surfaces.

Chem Commun (Camb)

Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Královopolská 135, 612 65, Brno, Czech Republic.

Published: April 2009

AI Article Synopsis

  • The study used constant current chronopotentiometry to analyze protein denaturation at a mercury electrode.
  • In a 50 mM sodium phosphate solution at pH 7, proteins like bovine serum albumin remained stable and did not denature.
  • However, at higher phosphate concentrations, the proteins experienced denaturation due to the influence of the electric field on the electrode surface.

Article 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.

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http://dx.doi.org/10.1039/b822274fDOI Listing

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