arXiv subjects

Tomás S. Plivelic

Publications and source records attributed to Tomás S. Plivelic.

4 recordsLinked to original sources

arXiv2026

Layered matter that maintains spacing but loses stacking order

In layered materials, spacing and stacking-order extent are usually locked. Here we show that in swollen suspensions of stiff, charged nanosheets they decouple, and that this defines a distinct regime, apart from the crystalline- and Wigner-swelling regimes such systems usually occupy. The mean spacing stays sharp and salinity-tunable while scattering-weighted stacking spans only two to three layers. We demonstrate this in a near-perfect model material, so the behaviour is intrinsic, not defect-driven. X-ray and neutron scattering, sedimentation and a Donnan analysis show the spacing is held by a parameter-free osmotic restoring slope below one pascal per nanometre. Because the slope is so weak, the spacing sits at equilibrium while faults relax slowly, a quenched metastable registry whose ageing-like relaxation of low-dimensional periodic order has not, to our knowledge, been realised before. The same decoupling is expected across stiff, swollen nanosheets, from clays to oxide nanosheets and graphene oxide.

cond-mat.soft↗

arXiv2026

Enhanced nanocomposite susceptibility by field-alignment of superparamagnetic particles

Nanocomposites comprised of insulated magnetic single-domain particles are promising candidates for high-frequency, eddy current free, soft magnetic materials, but tend to suffer from low magnetic susceptibility ($<20$). Particle alignment has been proposed to increase nanocomposite susceptibility and reduce magnetic losses but experimental verification has been lacking. Here, magnetic nanocomposites containing 3-57 vol\% field-aligned 11$\pm$3 nm maghemite particles in a poly-vinyl matrix were investigated for potential use as high-frequency inductor core materials. The particles were aligned by a homogenous static alignment field during nanocomposite drying, fixating the particle orientation. Particle aggregation was disproved by small-angle scattering. The dependence of the alignment field strength and particle concentration on the nanocomposite's susceptibility and hysteresis losses were investigated from DC up to 922 kHz by vibrating sample magnetometry, AC-susceptibility and high-frequency hysteresis measurements. Nanocomposite susceptibility increased super-linearly with particle fraction due to weak particle interactions. Alignment of the particles increased the nanocomposite susceptibility from 21 to 50 for samples with a particle content of 57 vol\%. Hence, the synergy between particle alignment and interaction allows for a higher than expected susceptibility of nanocomposites. The results show that magnetically aligning particles in a nanocomposite reduces magnetic losses when using well-dispersed single-domain superparamagnetic nanoparticles. Measured nanocomposite susceptibility could be modelled by a combination of directional dependent Debye-models including mean-field interaction effects and partial particle alignment. Measured susceptibility of 50 is among the highest obtained for nanocomposites, making it a relevant candidate for applications in power electronics.

physics.app-ph↗

arXiv2014

Weak self-interactions of globular proteins studied by small-angle X-ray scattering and structure-based modeling

We investigate protein-protein interactions in solution by small-angle X-ray scattering (SAXS) and theoretical modeling. The structure factor for solutions of bovine pancreatic trypsin inhibitor (BPTI), myoglobin (Mb), and intestinal fatty acid-binding protein (IFABP) is determined from SAXS measurements at multiple concentrations, from Monte Carlo simulations with a coarse-grained structure-based interaction model, and from analytic approximate solutions of two idealized colloidal interaction models without adjustable parameters. By combining these approaches, we find that the structure factor is essentially determined by hard-core and screened electrostatic interactions. Other soft short-ranged interactions (van der Waals and solvation-related) are either individually insignificant or tend to cancel out. The structure factor is also not significantly affected by charge fluctuations. For Mb and IFABP, with small net charge and relatively symmetric charge distribution, the structure factor is well described by a hard-sphere model. For BPTI, with larger net charge, screened electrostatic repulsion is also important, but the asymmetry of the charge distribution reduces the repulsion from that predicted by a charged hard-sphere model with the same net charge. Such charge asymmetry may also amplify the effect of shape asymmetry on the protein-protein potential of mean force.

physics.bio-ph↗

arXiv2014

Structure and kinetics of chemically cross-linked protein gels from small-angle X-ray scattering

Glutaraldehyde (GA) reacts with amino groups in proteins, forming intermolecular cross-links that, at sufficiently high protein concentration, can transform a protein solution into a gel. Although GA has been used as a cross-linking reagent for decades, neither the cross-linking chemistry nor the microstructure of the resulting protein gel have been clearly established. Here we use small-angle X-ray scattering (SAXS) to characterise the microstructure and structural kinetics of gels formed by cross-linking of pancreatic trypsin inhibitor, myoglobin or intestinal fatty acid-binding protein. By comparing the scattering from gels and dilute solutions, we extract the structure factor and the pair correlation function of the gels. The protein gels are spatially heterogeneous, with dense clusters linked by sparse networks. Within the clusters, adjacent protein molecules are almost in contact, but the protein concentration in the cluster is much lower than in a crystal. At the $\sim$1 nm SAXS resolution, the native protein structure is unaffected by cross-linking. The cluster radius is in the range 10 - 50 nm, with the cluster size determined mainly by the availability of lysine amino groups on the protein surface. The development of structure in the gel, on time scales from minutes to hours, appears to obey first-order kinetics. Cross-linking is slower at acidic pH, where the population of amino groups in the reactive deprotonated form is low. These results support the use of cross-linked protein gels in NMR studies of protein dynamics and for modeling NMR relaxation in biological tissue.

physics.chem-ph↗