In systems with small spin-orbit coupling, current-induced torques on the magnetization require inhomogeneous magnetization textures. For large spin-orbit coupling, such torques exist even without gradients in the magnetization direction. Here, we consider current-induced torques in ferromagnetic metals with both Rashba spin-orbit coupling and inhomogeneous magnetization. We first phenomenologically construct all torques that are allowed by the symmetries of the system, to first order in magnetization-direction gradients and electric field. Second, we use a Boltzmann approach to calculate the spin torques that arise to second order in the spin-orbit coupling. We apply our results to current-driven domain walls and find that the domain-wall mobility is strongly affected by torques that result from the interplay between spin-orbit coupling and inhomogeneity of the magnetization texture.

Ion mobility separates molecules in the gas-phase based on their physico-chemical properties, providing information about their size as collisional cross-sections. The timsTOF Pro combines trapped ion mobility with a quadrupole, collision cell and a time-of-flight mass analyzer, to probe ions at high speeds with on-the-fly fragmentation. Here, we show that on this platform ion mobility is beneficial for cross-linking mass spectrometry (XL-MS). Cross-linking reagents covalently link amino acids in close proximity, resulting in peptide pairs after proteolytic digestion. These cross-linked peptides are typically present at low abundance in the background of normal peptides, which can partially be resolved by using enrichable cross-linking reagents. Even with a very efficient enrichable cross-linking reagent, like PhoX, the analysis of cross-linked peptides is still hampered by the co-enrichment of peptides connected to a partially hydrolyzed reagent – termed mono-linked peptides. For experiments aiming to uncover protein-protein interactions these are unwanted byproducts. Here, we demonstrate that gas-phase separation by ion mobility enables the separation of mono-linked peptides from cross-linked peptide pairs. A clear partition between these two classes is observed at a CCS of 500 Å2 and a monoisotopic mass of 2 kDa, which can be used for targeted precursor selection. A total of 50 - 70% of the mono-linked peptides are prevented from sequencing, allowing the analysis to focus on sequencing the relevant cross-linked peptide pairs. In applications to both simple proteins and protein mixtures and a complete highly complex lysate this approach provides a substantial increase in detected cross-linked peptides.

Motivated by recent experiments by Lin et al., [Nature (London) 471, 83 (2011)] that engineered spin-orbit coupling in ultracold mixtures of bosonic atoms, we study the dipole oscillation of trapped spin-orbit-coupled noncondensed Bose and Fermi gases. We find that different directions of oscillation are coupled by the spin-orbit interactions. The phase difference between oscillatory motion in orthogonal directions and the trapping frequencies of the modes are shown to be related to the anomalous Hall conductivity. Our results can be used to experimentally determine the anomalous Hall conductivity for cold-atom systems.

Ion mobility separates molecules in the gas-phase on their physico-chemical properties, providing information about their size as collisional cross-sections. The timsTOF Pro combines trapped ion mobility with a quadrupole, collision cell and a time-of-flight mass analyzer, to probe ions at high speeds with on-the-fly fragmentation. Here, we show that on this platform ion mobility is beneficial for cross-linking mass spectrometry (XL-MS). Cross-linking reagents covalently link amino acids in close proximity, resulting in peptide pairs after proteolytic digestion. These cross-linked peptides are typically present at low abundance in the background of normal peptides, which can partially be resolved by using enrichable cross-linking reagents. Even with a very efficient enrichable cross-linking reagent, like PhoX, the analysis of cross-linked peptides is still hampered by the co-enrichment of peptides connected to a partially hydrolyzed reagent -termed mono-linked peptides. For experiments aiming to uncover protein-protein interactions these are unwanted byproducts. Here, we demonstrate that gas-phase separation by ion mobility enables the separation of mono-linked peptides from cross-linked peptide pairs. A clear partition between these two classes is observed at a CCS of 500Å 2 and a monoisotopic mass of 2 kDa, which can be used for targeted precursor selection. A total of 50 -70% of the mono-linked peptides are prevented from sequencing, allowing the analysis to focus on sequencing the relevant cross-linked peptide pairs. In applications to both simple proteins and protein mixtures and a complete highly complex lysate this approach provides a substantial increase in detected cross-linked peptides.