Tailoring the magnetism of Co atoms on graphene through substrate hybridization.

We determine the magnetic properties of individual Co atoms adsorbed on graphene (G) with x-ray absorption spectroscopy and magnetic circular dichroism. The magnetic ground state of Co adatoms strongly depends on the choice of the metal substrate on which graphene is grown. Cobalt atoms on G/Ru(0001) feature exceptionally large orbital and spin moments, as well as an out-of-plane easy axis with large magnetic anisotropy. Conversely, the magnetic moments are strongly reduced for Co/G/Ir(111), and the magnetization is of the easy-plane type. We demonstrate how the Co magnetic properties, which ultimately depend on the degree of hybridization between the Co 3d orbitals and graphene π bands, can be tailored through the strength of the graphene-substrate coupling.

Low temperature ferromagnetism in chemically ordered FeRh nanocrystals.

In sharp contrast to previous studies on FeRh bulk, thin films, and nanoparticles, we report the persistence of ferromagnetic order down to 3 K for size-selected 3.3 nm diameter nanocrystals embedded into an amorphous carbon matrix. The annealed nanoparticles have a B2 structure with alternating atomic Fe and Rh layers. X-ray magnetic dichroism and superconducting quantum interference device measurements demonstrate ferromagnetic alignment of the Fe and Rh magnetic moments of 3 and 1µ(B), respectively. The ferromagnetic order is ascribed to the finite-size induced structural relaxation observed in extended x-ray absorption spectroscopy.

The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function.

The superantigens staphylococcal enterotoxin A and E (SEA and SEE) can activate a large number of T-cells. SEA and SEE have approximately 80% sequence identity but show some differences in their biological function. Here, the two superantigens and analogues were characterized biophysically. SEE was shown to have a substantially higher thermal stability than SEA. Both SEA and SEE were thermally stabilized by 0.1 mM Zn(2+) compared with Zn(2+)-reduced conditions achieved using 1 mM EDTA or specific replacements that affect Zn(2+) coordination. The higher stability of SEE was only partly caused by the T-cell receptor (TCR) binding regions, whereas regions in the vicinity of the major histocompatibility complex class II binding sites affected the stability to a greater extent. SEE exhibited a biphasic denaturation between pH 5.0-6.5, influenced by residues in the TCR binding regions. Interestingly, enzyme-linked immunosorbent assay, isoelectric focusing, and circular dichroism analysis indicated that conformational changes had occurred in the SEA/E chimerical constructs relative to SEA and SEE. Thus, it is proposed that the Zn(2+) binding site is very important for the stability and potency of SEA and SEE, whereas residues in the TCR binding site have a substantial influence on the molecular conformation to control specificity and function.