We investigate the process of selectively manipulating the magnetization alignment in magnetic layers in the Fe/GaAs/GaMnAs structure by current-induced spin-orbit (SO) magnetic field. The presence of such fields manifests itself through the hysteretic behavior of planar Hall resistance observed for two opposite currents as the magnetization in the structure switches directions. In the case of the Fe/GaAs/GaMnAs multilayer, hystereses are clearly observed when the magnetization switches direction in the GaMnAs layer, but are negligible when magnetization transitions occur in Fe. This difference in the effect of the SO-field in the two magnetic layers provides an opportunity to control the magnetization in one layer (in the presence case in GaMnAs) by a current, while the magnetization in the other layer (i.e., Fe) remains fixed. Owing to our ability to selectively control the magnetization in the GaMnAs layer, we are able to manipulate the relative spin configurations in our structure between collinear and non-collinear alignments simply by switching the current direction even in the absence of an external magnetic field.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5578966 | PMC |
http://dx.doi.org/10.1038/s41598-017-10621-6 | DOI Listing |
Anal Chem
January 2025
Institute for Bioengineering of Catalonia (IBEC), Barcelona Institute of Science and Technology (BIST), 08028 Barcelona, Spain.
Nuclear magnetic resonance (NMR) spectroscopy is a valuable diagnostic tool limited by low sensitivity due to low nuclear spin polarization. Hyperpolarization techniques, such as dissolution dynamic nuclear polarization, significantly enhance sensitivity, enabling real-time tracking of cellular metabolism. However, traditional high-field NMR systems and bioreactor platforms pose challenges, including the need for specialized equipment and fixed sample volumes.
View Article and Find Full Text PDFJ Med Chem
January 2025
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111Budapest, Hungary.
The binding ability of human serum albumin (HSA) on active pharmaceutical ingredients (APIs) is one of the most important parameters in the early stages of drug discovery. In this study, an immobilized HSA-based tool was developed for the rapid and easy in vitro screening of API binding. The work explored the serious incompleteness in the identification of HSA used for in vitro screening published in the last five years.
View Article and Find Full Text PDFPurpose: To create tridimensional (3D) anatomical models of diaphyseal fractures in dogs (3D AMDFD) and to evaluate the models from their radiographs.
Methods: The study consisted of six stages: preparation of femur from a healthy dog cadaver; digitalization of the bone through a 3D scanner and creation of the base model; creation of a 3D AMDFD based on the image of the base model, 3D modeling carried out to reproduce five different types of diaphyseal fractures; printing the models produced on a 3D printer with a thermoplastic material; insertion of neodymium magnets in the fracture line to allow the assembly and disassembly of the parts; and radiography of 3D AMDFD in lateromedial and craniocaudal positions.
Results: The base model and 3D AMDFD had high precision in the replication of bone structures, like the bone in natura.
J Am Chem Soc
January 2025
Department of Chemistry, 1102 Natural Sciences II, University of California, Irvine, California 92697, United States.
The development of molecular species with switchable magnetic properties has been a long-standing challenge in chemistry. One approach involves binding an analyte, such as protons, to a compound to trigger a change in magnetism. Transition metal complexes have been targeted for this type of magnetic modulation because they can undergo changes in their spin states.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!