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Magnetic nanopatterns were successfully created in FeRh thin film deposited on MgO (100) substrates. Silica and polystyrene spherical masks, nominally 500 and 1000 nm in diameter, respectively were applied on the surface of the sample in order to locally shadow the film against the effect of 110 keV energy neon-ion irradiation with fluences of 1015 and 1016 ions/cm2. Such nanosphere-lithography technique allows for projecting the mask geometry on the magnetic structure of the FeRh film. Conversion-electron Mössbauer spectroscopy and magnetic force microscopy were used to determine the ferromagnetic ratio and the magnetic pattern in the samples, and nuclear resonance scattering of synchrotron radiation was applied to obtain the in-depth magnetic profile. From the results obtained, the possible three-dimensional (3D) structure of the created individual magnetic domains was also constructed. Overall, the great customizability of the presented nanosphere-lithography technique in FeRh thin film provides opportunities for developing cutting-edge spintronic applications. [ABSTRACT FROM AUTHOR]

A 10 kDa dynein light chain (DLC), previously identified as a tail light chain of myosin Va, may function as a cargo-binding and/or regulatory subunit of both myosin and dynein. Here, we identify and characterize the binding site of DLC on myosin Va. Fragments of the human myosin Va tail and the DLC2 isoform were expressed, and their complex formation was analyzed by pull-down assays, gel filtration, and spectroscopic methods. DLC2 was found to bind as a homodimer to a ~15 residue segment (11e1280-11e1294) localized between the medial and distal coiled-coil domains of the tail. The binding region contains the three residues coded by the alternatively spliced exon B (Asp 1284-Lys 1286). Removal of exon B eliminates DLC2 binding. Co-localization experiments in a transfected mammalian cell line confirm our finding that exon B is essential for DLC2 binding. Using circular dichroism, we demonstrate that binding of DLC2 to a ~85 residue disordered domain (Pro1235-Arg1320) induces some helical structure and stabilizes both flanking coiled-coil domains (melting temperature increases by ~7 °C). This result shows that DLC2 promotes the assembly of the coiled-coil domains of myosin Va. Nuclear magnetic resonance spectroscopy and docking simulations show that a 15 residue peptide (Ile1280-Ile1294) binds to the surface grooves on DLC2 similarly to other known binding partners of DLCs. When our data are taken together, they suggest that exon B and its associated DLC2 have a significant effect on the structure of parts of the coiled-coil tail domains and such a way could influence the regulation and cargo-binding function of myosin Va. [ABSTRACT FROM AUTHOR]