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magnetochemistryArticleRevisiting the Possible Functionality of the MagR ProteinAlexander Pekarsky 1 , Herwig Michorand Oliver Spadiut 1, Institute of Chemical, Environmental and Bioscience Engineering, Study Area Biochemical Engineering, TU Wien, 1060 Wien, Austria; [email protected] Institute of Strong State Physics, TU Wien, 1040 Wien, Austria; [email protected] Correspondence: [email protected]: Current findings have sparked good interest within the putative magnetic receptor protein MagR. However, in vivo experiments have revealed no magnetic moment of MagR at space temperature. Nevertheless, the interaction of MagR and MagR fusion Nimbolide web proteins with silica-coated magnetite beads have established beneficial for protein purification. Within this study, we recombinantly produced two diverse MagR proteins in Escherichia coli BL21(DE3) to (1) expand earlier protein purification research, (two) test if MagR can magnetize whole E. coli cells when it can be expressed to a higher cytosolic, soluble titer, and (3) investigate the MagR-expressing E. coli cells’ magnetic properties at low temperatures. Our benefits show that MagR induces no measurable, permanent magnetic moment in cells at low temperatures, indicating no usability for cell magnetization. Furthermore, we show the limited usability for magnetic bead-based protein purification, hence closing the present expertise gap among theoretical considerations and empirical information on the MagR protein. Keywords and phrases: magnetic receptor protein (MagR); Escherichia coli; magnetism; affinity chromatography; SQUIDCitation: Pekarsky, A.; Michor, H.; Spadiut, O. Revisiting the Prospective Functionality on the MagR Protein. Magnetochemistry 2021, 7, 147. https://doi.org/10.3390/ magnetochemistry7110147 Academic Editor: Kevin Bernot Received: 20 October 2021 Accepted: 9 November 2021 Published: 11 November1. Compound 48/80 web Introduction Iron ulfur (Fe ) cluster proteins are vital for various physiological processes and are present in most recognized prokaryotic and eukaryotic cells [1]. The iron atoms in [2FeS] clusters have already been reported to interact through antiferromagnetic coupling [4]. Only recently, the Fe cluster protein MagR (magnetic receptor) came into spotlight [5]. The authors proposed a possible answer to the query on navigation of migratory animals. They reported that MagR, a compact ( 14 kDa) [2FeS] protein from pigeons with homologs in many species, forms a ferrimagnetic, multimeric complex that responds to magnetic fields in vitro. Qin et al. also showed that the MagR protein and also a MagR/Cryptochrome complicated can be isolated and enriched from a complex matrix by silica-coated magnetite (SiO2 e3 O4 ) beads [5]. Later, MagR fusion proteins have been successfully captured from a complex matrix [6,7]. Given that its discovery, the physical capabilities of MagR have been intensively questioned. When MagR constructs have been subjected to magnetic stimuli in mammalian cells, they were not able to induce significant membrane channel activity in a magnetic field [8], in contrast to earlier final results [9]. The biologist Markus Me.
