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J Phys Chem B. 2015 Oct 1;119(39):12561-7. doi: 10.1021/acs.jpcb.5b04952. Epub 2015 Sep 16.

Formation of Organized Protein Thin Films with External Electric Field.

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PIPE, Federal University of Paraná , Centro Politécnico - Adm. Building, 2° Floor, 81531-990 Curitiba, Paraná, Brazil.
Biochemistry and Molecular Biology, Federal University of Paraná , P.O. Box 19046, 81531-990 Curitiba, Paraná, Brazil.


The effect of an external electric field on the formation of protein GlnB-Hs films and on its buffer solution on siliconized glass slides has been analyzed by current versus electric field curves and atomic force microscopy (AFM). The Herbaspirillum seropedicae GlnB protein (GlnB-Hs) is a globular, soluble homotrimer (36 kDa) with its 3-D structure previously determined. Concentrations of 10 nM native denatured GlnB-Hs protein were deposited on siliconized glass slides under ambient conditions. Immediately after solution deposition a maximum electric field of 30 kV/m was applied with rates of 3 V/s. The measured currents were surface currents and were analyzed as transport current. Electric current started to flow only after a minimum electric field (critical value) for the systems analyzed. The AFM images showed films with a high degree of directional organization only when the proteins were present in the solution. These results showed that the applied electric field favored directional organization of the protein GlnB-Hs films and may contribute to understand the formation of protein films under applied electric fields.

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