Ferromagnetic resonance of a two-dimensional array of nanomagnets: Effects of surface anisotropy and dipolar interactions

We develop an analytical approach for studying the FMR frequency shift due to dipolar interactions and surface effects in two-dimensional arrays of nanomagnets with (effective) uniaxial anisotropy along the magnetic field. For this we build a general formalism on the basis of perturbation theory that applies to dilute assemblies but which goes beyond the point-dipole approximation as it takes account of the size and shape of the nano-elements, in addition to their separation and spatial arrangement. The contribution to the frequency shift due to the shape and size of the nano-elements has been obtained in terms of their aspect ratio, their separation and the lattice geometry. We have also varied the size of the array itself and compared the results with a semi-analytical model and reached an agreement that improves as the size of the array increases. We find that the red-shift of the ferromagnetic resonance due to dipolar interactions decreases for smaller arrays. Surface effects may induce either a blue-shift or a red-shift of the FMR frequency, depending on the crystal and magnetic properties of the nano-elements themselves. In particular, some configurations of the nano-elements assemblies may lead to a full compensation between surface effects and dipole interactions.Comment: 14 pages, 5 figure

Dynamics of a magnetic dimer with exchange, dipolar and Dzyalozhinski-Moriya interaction

We investigate the dynamics of a magnetic system consisting of two magnetic moments coupled by either exchange, dipole-dipole, or Dzyalozhinski-Moriya interaction. We compare the switching mechanisms and switching rates as induced by the three couplings. For each coupling and each configuration of the two anisotropy axes, we describe the switching modes and, using the kinetic theory of Langer, we provide (semi-)analytical expressions for the switching rate. We then compare the three interactions with regard to their efficiency in the reversal of the net magnetic moment of the dimer. We also investigate how the energy barriers vary with the coupling. For the dipole-dipole interaction we find that the energy barrier may either increase or decrease with the coupling depending on whether the latter is weak or strong. Finally, upon comparing the various switching rates, we find that the dipole-dipole coupling leads to the slowest magnetic dimer, as far as the switching of its net magnetic moment is concerned.Comment: 20 pages, 18 Figures, 2 table

Stochastic thermodynamics of holonomic systems

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SMCHD1 is involved in de novo methylation of the DUX4-encoding D4Z4 macrosatellite

The DNA methylation epigenetic signature is a key determinant during development. Rules governing its establishment and maintenance remain elusive especially at repetitive sequences, which account for the majority of methylated CGs. DNA methylation is altered in a number of diseases including those linked to mutations in factors that modify chromatin. Among them, SMCHD1 (Structural Maintenance of Chromosomes Hinge Domain Containing 1) has been of major interest following identification of germline mutations in Facio-Scapulo-Humeral Dystrophy (FSHD) and in an unrelated developmental disorder, Bosma Arhinia Microphthalmia Syndrome (BAMS). By investigating why germline SMCHD1 mutations lead to these two different diseases, we uncovered a role for this factor in de novo methylation at the pluripotent stage. SMCHD1 is required for the dynamic methylation of the D4Z4 macrosatellite upon reprogramming but seems dispensable for methylation maintenance. We find that FSHD and BAMS patient's cells carrying SMCHD1 mutations are both permissive for DUX4 expression, a transcription factor whose regulation has been proposed as the main trigger for FSHD. These findings open new questions as to what is the true aetiology for FSHD, the epigenetic events associated with the disease thus calling the current model into question and opening new perspectives for understanding repetitive DNA sequences regulation

Probing and quantifying DNA–protein interactions with asymmetrical flow field-flow fractionation

Tools capable of measuring binding affinities as well as amenable to downstream sequencing analysis are needed for study of DNA-protein interaction, particularly in discovery of new DNA sequences with affinity to diverse targets. Asymmetrical flow field-flow fractionation (AF4) is an open-channel separation technique that eliminates interference from column packing to the non-covalently bound complex and could potentially be applied for study of macromolecular interaction. The recovery and elution behaviors of the poly(dA)n strand and aptamers in AF4 were investigated. Good recovery of ssDNAs was achieved by judicious selection of the channel membrane with consideration of the membrane pore diameter and the radius of gyration (Rg) of the ssDNA, which was obtained with the aid of a Molecular Dynamics tool. The Rg values were also used to assess the folding situation of aptamers based on their migration times in AF4. The interactions between two ssDNA aptamers and their respective protein components were investigated. Using AF4, near-baseline resolution between the free and protein-bound aptamer fractions could be obtained. With this information, dissociation constants of ∼16nM and ∼57nM were obtained for an IgE aptamer and a streptavidin aptamer, respectively. In addition, free and protein-bound IgE aptamer was extracted from the AF4 eluate and amplified, illustrating the potential of AF4 in screening ssDNAs with high affinity to targets. Our results demonstrate that AF4 is an effective tool holding several advantages over the existing techniques and should be useful for study of diverse macromolecular interaction systems