Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros

Base de dados
País/Região como assunto
Tipo de documento
País de afiliação
Intervalo de ano de publicação
1.
Phys Rev Lett ; 128(19): 197202, 2022 May 13.
Artigo em Inglês | MEDLINE | ID: mdl-35622053

RESUMO

Current-induced spin torques provide efficient data writing approaches for magnetic memories. Recently, the spin splitting torque (SST) was theoretically predicted, which combines advantages of conventional spin transfer torque (STT) and spin-orbit torque (SOT) as well as enables controllable spin polarization. Here we provide the experimental evidence of SST in collinear antiferromagnet RuO_{2} films. The spin current direction is found to be correlated to the crystal orientation of RuO_{2} and the spin polarization direction is dependent on (parallel to) the Néel vector. These features are quite characteristic for the predicted SST. Our finding not only presents a new member for the spin torques besides traditional STT and SOT, but also proposes a promising spin source RuO_{2} for spintronics.

3.
J Dairy Sci ; 90(11): 5004-11, 2007 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-17954739

RESUMO

Bovine casein was digested with pepsin at pH 2.0 in a batch-stirred tank reactor. To investigate the effect of peptic digestion on the aggregate size and molecular weight distribution of bovine casein, the resulting hydrolysates were examined by size-exclusion chromatography coupled with multiangle laser light scattering and dynamic light scattering. Casein was resolved by size-exclusion chromatography into 2 major peaks corresponding to aggregates and monomers, both of which showed a continuous decrease as hydrolysis proceeded. However, the ratio of aggregates to monomers was maintained at almost 1 (2:2.5) during the initial 30-min hydrolysis, indicating that the caseins in solution were in a type of equilibrium between aggregates and monomers. Upon peptic hydrolysis, casein aggregates increased in size and molecular weight, and exhibited a decrease in intermolecular repulsion. This finding was confirmed by dynamic light scattering measurements, which traced the changes in the hydrodynamic radii and light scattering intensities of casein hydrolysates. In addition, the release kinetics of peptide fractions with different molecular weights was also examined. It was concluded that the increase in hydrophobic attraction and the reduction in intermicellar repulsion might promote the growth in aggregate size of bovine casein during the limited hydrolysis.


Assuntos
Caseínas/química , Caseínas/metabolismo , Pepsina A/metabolismo , Animais , Bovinos , Cromatografia em Gel/métodos , Hidrólise , Peso Molecular , Hidrolisados de Proteína/química , Padrões de Referência
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA