Tuning protein GlnB-Hs surface interaction with silicon: FTIR-ATR, AFM and XPS study

[Display omitted] ► Thin films of GlnB-Hs protein were prepared on hydrophilic and hydrophobic silicon. ► GlnB-Hs is adsorbed face-up on hydrophilic silicon deprotonating its residues. ► On hydrophobic silicon, GlnB-Hs forms filaments adopting side-on conformation. ► GlnB-Hs secondary structure was...

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Veröffentlicht in:	Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2013-02, Vol.102, p.348-353
Hauptverfasser:	Lubambo, A.F., Benelli, E.M., Klein, J.J., Schreiner, W.H., Silveira, E., de Camargo, P.C.
Format:	Artikel
Sprache:	eng
Schlagworte:	adsorption atomic force microscopy Bacterial Proteins - chemistry Bacterial Proteins - metabolism carbon coatings colloids Electrostatic interactions Fourier transform infrared spectroscopy GlnB Herbaspirillum - metabolism Herbaspirillum seropedicae hydrophilicity Hydrophobic and Hydrophilic Interactions hydrophobicity metabolism Microscopy, Atomic Force - methods nitrogen Photoelectron Spectroscopy - methods Protein adsorption Protein Binding Protein secondary structure Protein Structure, Secondary Protein–surface interactions reflectance spectroscopy signal transduction Silicon Silicon - chemistry Spectroscopy, Fourier Transform Infrared - methods Static Electricity X-ray photoelectron spectroscopy
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