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1.
Opt Express ; 31(20): 32582-32590, 2023 Sep 25.
Article in English | MEDLINE | ID: mdl-37859058

ABSTRACT

This paper presents the demonstration of an on-chip integrated terahertz (THz) apodized Bragg grating (TABG) which functions as band-stop filter with a center frequency of 0.8 THz and a bandwidth of 200 GHz. For experimentation, we integrate the TABG into our THz system-on-chip to enable wideband (DC - 1.5 THz) device characterization. Using this methodology, we measure the signal transmission through the TABG and find the experimental results align with simulation and theory provides a rejection of approximately 20 dB across the stop-band.

2.
Mol Biotechnol ; 61(1): 12-19, 2019 Jan.
Article in English | MEDLINE | ID: mdl-30443852

ABSTRACT

Recombinant flagellin (FliC) has shown low efficacy in purification because of inclusion bodies formation and aggregation. We hypothesized preserving TLR5 binding site of FliC and removing some amino acids could be responsible for aggregation and solubility improvement. Hence, a bioinformatics study was performed to find hotspots in aggregate formation. Protein modeling was carried out by SWISS-MODEL and I-TASSER servers and models were compared by MATRAS server and Chimera 1.11.2. Gene modification was carried out based on bioinformatics studies. Genes, (truncated modified fliC (tmFliC) and full-length fliC (flFliC)), were cloned and expressed in pET-21a vector. Protein purification was carried out using HIS-Tag method. Proliferation assay and also induction of IL-8 in HEK293 cells were performed to confirm bioactivity function of tmFliC. Bioinformatics results showed that partial deletion of C-terminus may increase solubility without unfavorable effect on TLR5 recognition. Also, model comparison showed that this protein may preserve 3D structure. In addition, GlobPlot server demonstrated that tmFliC formed its globular domains which were important in TLR5 recognition. As we expected, high purification efficacy for tmFliC compared with flFliC was also obtained in experimental studies and a proper function for tmFliC was observed. The tmFliC enhanced cell proliferation in HEK293 cells compare with control after 24 h. Also, IL-8 level was increased with stimulation by tmFliC after 24 h. In conclusion, reducing hydrophobicity in C-terminus and deleting necessary amino acids for filament formation may increase protein solubility.


Subject(s)
Bacterial Proteins , Flagellin , Recombinant Fusion Proteins , Salmonella typhimurium/genetics , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Cell Proliferation , Computational Biology , Escherichia coli/genetics , Flagellin/chemistry , Flagellin/genetics , Flagellin/isolation & purification , Flagellin/metabolism , HEK293 Cells , Humans , Models, Molecular , Protein Engineering , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/isolation & purification , Recombinant Fusion Proteins/metabolism
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