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| http://dx.doi.org/10.3389/fphar.2020.625662 | DOI Listing |
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Calprotectin's Protein Structure Shields Ni-N(His) Bonds from Competing Agents.
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State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.
The Ni-N(His) coordination bond, formed between the nickel ion and histidine residues, is essential for recombinant protein purification, especially in Ni-NTA-based systems for selectively binding polyhistidine-tagged (Histag) proteins. While previous studies have explored its bond strength in a synthetic Ni-NTA-Histag system, the influence of the surrounding protein structure remains less understood. In this study, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to quantify the Ni-N(His) bond strength in calprotectin, a biologically relevant protein system.
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Department of Psychiatry and Behavioral Health, Penn State College of Medicine, Hershey, PA, USA.
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View Article and Find Full Text PDFExploring ferroptosis and miRNAs: implications for cancer modulation and therapy.
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Department of Molecular Genetics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box: 14115-154, Tehran, Iran.
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View Article and Find Full Text PDFThe potential of alphapinene as a therapeutic agent for maternal hypoxia-induced cognitive impairments: a study on HO-1 and Nrf2 gene expression in rats.
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Department of Biochemistry and Molecular Biology, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
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