1. Tuning protein GlnB-Hs surface interaction with silicon: FTIR-ATR, AFM and XPS study
- Author
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Lubambo, A.F., Benelli, E.M., Klein, J.J., Schreiner, W.H., Silveira, E., and de Camargo, P.C.
- Subjects
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NANOSILICON , *PROTEIN analysis , *CELLULAR signal transduction , *HYDROPHOBIC surfaces , *ADSORPTION (Chemistry) , *FOURIER transform infrared spectroscopy , *ATOMIC force microscopy - Abstract
Abstract: Herbaspirillum seropedicae GlnB (GlnB-Hs) is a signal transduction protein involved in the control of nitrogen, carbon and energetic metabolism. The adsorption of GlnB-Hs deposited by spin coating on hydrophilic and hydrophobic silicon forms a thin layer that was characterized using atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS) and Fourier transform infrared attenuated total reflectance spectroscopy (FTIR-ATR). AFM allowed the identification of globular, face-up donut like array of protein on hydrophilic silicon substrate, favoring deprotonated residues to contact the silicon oxide surface. Over hydrophobic silicon, GlnB-Hs adopts a side-on conformation forming a filament network, avoiding the contact of protonated residues with silicon surface. XPS allowed us to determine the protonated and non-protonated states of nitrogen 1s (N 1s). The FTIR-ATR measurements provided information about protein secondary structure and its conservation, after surface adsorption. [Copyright &y& Elsevier]
- Published
- 2013
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