The present article recapitulates the development of the polyhistidine affinity tag purification principle. Emphasis is laid on events behind the scenes which were never published. The key concept of the method emerged in a team discussion and its further development was driven by the need of Roche in-house projects.
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http://dx.doi.org/10.2533/chimia.2020.363 | DOI Listing |
Int J Mol Sci
December 2024
Institute of Food Technology, Department of Food Science and Technology, BOKU University, 1190 Vienna, Austria.
is a potential bacterial cell factory to develop delivery systems for vaccines and therapeutic proteins. Much progress has been made in applications using engineered against, e.g.
View Article and Find Full Text PDFProtein Sci
January 2025
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, USA.
After overexpression in a suitable host, recombinant protein purification often relies on affinity (e.g., poly-histidine) and solubility-enhancing (e.
View Article and Find Full Text PDFJ Chromatogr A
September 2024
School of Product Design, University of Canterbury, Private Bag 4800, Christchurch 8020, New Zealand; Biomolecular Interaction Centre, University of Canterbury, Private Bag 4800, Christchurch 8020, New Zealand. Electronic address:
Dalton Trans
August 2024
College of Chemistry and Chemical Engineering, Shanghai University of Engineering Science, Shanghai 201620, China.
A new type of hybrid material (NCMTs@MoO/FeNi) with a multi-layer heterostructure was designed and fabricated a one-step pyrolysis process using FeOOH/NiMoO@PDA as the precursor. FeOOH/NiMoO@PDA was prepared by the solvothermal method, followed by the nickel-ion etching method coupled with the polymerization of dopamine (DA). The as-obtained material was made of nitrogen-doped carbon nanotubes embedded with FeNi and MoO nanoparticles (NPs).
View Article and Find Full Text PDFJ Mol Biol
August 2024
Department of Microbiology, University of Alabama at Birmingham Heersink School of Medicine, Birmingham, AL, USA. Electronic address:
In Escherichia coli, many environmental stressors trigger polyphosphate (polyP) synthesis by polyphosphate kinase (PPK1), including heat, nutrient restriction, toxic compounds, and osmotic imbalances. PPK1 is essential for virulence in many pathogens and has been the target of multiple screens for small molecule inhibitors that might serve as new anti-virulence drugs. However, the mechanisms by which PPK1 activity and polyP synthesis are regulated are poorly understood.
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