Effect of protein solution components in the adsorption of Herbaspirillum seropedicae GlnB protein on mica

Ferreira, Cecília F.G.; Benelli, Elaine Machado; Klein, J. J.; Schreiner, W. H.; Camargo, P.C. de

doi:10.1016/j.colsurfb.2009.05.034

Cited by 3 publications

(6 citation statements)

References 16 publications

(21 reference statements)

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“…Electric-Field Effects on Native GlnB-Hs Protein Films Formed on Silicone Channels. In previous experiments, native GlnB-Hs protein solution when dispensed directly onto solid surfaces by drop deposition showed selforganization in doughnut-like structures, for both bare mica 24 and hydrophilic silicon surface, contrasting with filamentary structures formed on hydrophobic Si surface. 25 Similarly, films of native GlnB-Hs formed by drop deposition on siliconized glass slides also formed doughnut-like supramolecular structures (132 ± 18 nm wide), indicated by arrows in the Figure 2A, which were randomly distributed on the surface.…”

Section: Resultsmentioning

confidence: 89%

“…Ferreira et al 24 showed that buffer compounds also formed globular supramolecular structures on mica when deposited by drop deposition. 24 These globular shapes can induce misleading interpretation of AFM images due to the similarities between the structures formed by buffer compounds and those of protein origin (Figure 3).…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Gln B -Hs protein films were previously analyzed with atomic force microscopy (AFM) and XPS spectroscopy in different hydrophobics substrates and in different kinds of procedures. , The supramolecular structures formed by protein Gln B -Hs are dependent on buffer solution and deposition method. Ferreira et al showed that the self-organized protein changed with salt concentration onto bare mica and possible artifacts due to salt contribution. Thin films of Gln B -Hs protein formed on hydrophilic and hydrophobic silicon (1 1 1) and (1 0 0) surface were investigated by AFM and XPS by Lubambo et al., showing self-organization doughnut-like structures on hydrophilic silicon surface and in filaments on hydrophobic Si surface …”

Section: Introductionmentioning

confidence: 99%

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Formation of Organized Protein Thin Films with External Electric Field

2015

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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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Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Formation of Organized Protein Thin Films with External Electric Field

2015

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“…Once the buffer compounds form similar structures in drop deposition films, , AFM images have been taken from thin films formed by buffer solution exposed to EEF. These images showed no evidence of orientation and a random distribution of buffer compounds (Figures c,f and c,f), similar to the pattern seen in the drop deposition protein films.…”

Section: Resultsmentioning

confidence: 99%

Use of Protein Thin Film Organized by External Electric Field as a Template for Protein Crystallization

Walter

Ferreira²,

Iulek

et al. 2018

ACS Omega

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The well-known difficulty to obtain high-quality protein crystals has motivated researchers to come up with new methods or modifications of established crystallization methods to stimulate the growth of good diffracting crystals. In the present work, a new approach, using a protein thin film organized by external electric field (EEF) as a template for protein crystal growth, is introduced. This method increased nucleation of hen egg white lysozyme (HEWL) in comparison with the classical vapor diffusion method, besides improving crystal morphology and size. X-ray diffraction analyses indicated improvements in crystal quality. When HEWL was crystallized at pH 6.2, in which this protein presents biological activity, the control crystal presented a poorly ordered crystalline structure and a low resolution cutoff at 3.42 Å, whereas the crystal grown with the EEF protein film revealed a high-resolution limit at 1.67 Å. These results suggest that protein films organized by EEF may improve protein crystals and their data quality.

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Review on the applications of atomic force microscopy imaging in proteins

Gao

Wang

et al. 2022

Micron

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Effect of protein solution components in the adsorption of Herbaspirillum seropedicae GlnB protein on mica

Cited by 3 publications

References 16 publications

Formation of Organized Protein Thin Films with External Electric Field

Formation of Organized Protein Thin Films with External Electric Field

Use of Protein Thin Film Organized by External Electric Field as a Template for Protein Crystallization

Review on the applications of atomic force microscopy imaging in proteins

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