Temperature-Dependent Spin Transport and Current-Induced Torques in Superconductor-Ferromagnet Heterostructures.

We investigate the injection of quasiparticle spin currents into a superconductor via spin pumping from an adjacent ferromagnetic metal layer. To this end, we use NbN-Ni_{80}Fe_{20}(Py) heterostructures with a Pt spin sink layer and excite ferromagnetic resonance in the Permalloy layer by placing the samples onto a coplanar waveguide. A phase sensitive detection of the microwave transmission signal is used to quantitatively extract the inductive coupling strength between the sample and the coplanar waveguide, interpreted in terms of inverse current-induced torques, in our heterostructures as a function of temperature. Below the superconducting transition temperature T_{c}, we observe a suppression of the dampinglike torque generated in the Pt layer by the inverse spin Hall effect, which can be understood by the changes in spin current transport in the superconducting NbN layer. Moreover, below T_{c} we find a large fieldlike current-induced torque.

Observation of Antiferromagnetic Magnon Pseudospin Dynamics and the Hanle Effect.

We report on experiments demonstrating coherent control of magnon spin transport and pseudospin dynamics in a thin film of the antiferromagnetic insulator hematite utilizing two Pt strips for all-electrical magnon injection and detection. The measured magnon spin signal at the detector reveals an oscillation of its polarity as a function of the externally applied magnetic field. We quantitatively explain our experiments in terms of diffusive magnon transport and a coherent precession of the magnon pseudospin caused by the easy-plane anisotropy and the Dzyaloshinskii-Moriya interaction. This experimental observation can be viewed as the magnonic analog of the electronic Hanle effect and the Datta-Das transistor, unlocking the high potential of antiferromagnetic magnonics toward the realization of rich electronics-inspired phenomena.

Angle Resolved Relaxation of Spin Currents by Antiferromagnets in Spin Valves.

We observe and analyze tunable relaxation of a pure spin current by an antiferromagnet in spin valves. This is achieved by carefully controlling the angle between a resonantly excited ferromagnetic layer pumping the spin current and the Néel vector of the antiferromagnetic layer. The effect is observed as an angle-dependent spin-pumping contribution to the ferromagnetic resonance linewidth. An interplay between spin-mixing conductance and, often disregarded, longitudinal spin conductance is found to underlie our observations, which is in agreement with a recent prediction for related ferromagnetic spin valves.

A colorimetric procedure to monitor the extent of crosslinking of proteins by bisimidoesters.

Reaction of proteins with bisimidoesters is one of the popular crosslinking techniques. The extent of the reaction cannot be followed directly using the commonly used free amino group-determining reagents ninhydrin and 2,4,6-trinitrobenzene sulfonic acid since they react with bisimidoesters. However, we found that the extent of amidination of protein could be followed colorimetrically by using 1-fluoro-2,4-dinitrobenzene.

Crosslinking of concanavalin A with glutaraldehyde.

Crosslinking of Concanavalin A with low concentrations of glutaraldehyde gives a mixture of products. A specific product having about 66% of the biological activity of the native molecule was characterized. Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis showed the presence of monomers, dimers, trimers, tetramers, and a small amount of pentamers as products. The presence of alpha-methyl mannoside during crosslinking changed the nature of the products, yielding a product retaining 80% of the biological activity. The crosslinked products showed greater stability than the native molecule at alkaline pH. However, the greatest stability under alkaline conditions was shown by the native molecule itself where alpha-methyl mannoside was present.

Crosslinked concanavalin A-O-(diethylaminoethyl)-cellulose--an affinity medium for concanavalin A-interacting glycoproteins.

When concanavalin A (Con A) is reacted with a low concentration of glutaraldehyde, the product formed strongly binds to DEAE-cellulose. Thus, the resultant material can be used as an affinity medium for those glycoproteins which interact with Con A. This affinity medium is easy to prepare, has a capacity comparable to that of similar commercially available affinity media, and is stable for up to at least 6 months.