Magnetic circular dichroism in two-photon photoemission.

We report the observation of magnetic circular dichroism (MCD) in two-photon photoemission (2PPE). The Heusler alloys Ni2MnGa and Co2FeSi were investigated by excitation with femtosecond laser light, showing MCD asymmetries of A=(3.5+/-0.5)x10;{-3} for Ni2MnGa and of A=(2.1+/-1.0)x10;{-3} for Co2FeSi, respectively. A theoretical explanation is provided based on local spin-density calculations for the magnetic dichroic response; the computed 2PPE MCD agrees well with the experiment. The observed 2PPE magnetic contrast represents an interesting alternative for future time-resolved photoemission studies on surface magnetism practicable in the laboratory.

Hidden order in URu2Si2 originates from Fermi surface gapping induced by dynamic symmetry breaking.

Spontaneous, collective ordering of electronic degrees of freedom leads to second-order phase transitions that are characterized by an order parameter driving the transition. The notion of a 'hidden order' has recently been used for a variety of materials where a clear phase transition occurs without a known order parameter. The prototype example is the heavy-fermion compound URu(2)Si(2), where a mysterious hidden-order transition occurs at 17.5 K. For more than twenty years this system has been studied theoretically and experimentally without a firm grasp of the underlying physics. Here, we provide a microscopic explanation of the hidden order using density-functional theory calculations. We identify the Fermi surface 'hot spots' where degeneracy induces a Fermi surface instability and quantify how symmetry breaking lifts the degeneracy, causing a surprisingly large Fermi surface gapping. As the mechanism for the hidden order, we deduce spontaneous symmetry breaking through a dynamic mode of antiferromagnetic moment excitations.

Calculated magneto-optical Kerr spectra of the half-Heusler compounds AuMnX (X = In, Sn, Sb).

The ferromagnetic ground states of the half-Heusler compounds AuMnX (X = In, Sn, Sb) have been calculated in the framework of the local spin-density approximation (LSDA) to density functional theory (DFT). AuMnSn is computed to be a half-metallic ferromagnet, whereas AuMnIn and AuMnSb are not half-metallic, due to their different band filling. The computed relativistic electronic structures served as inputs to calculate the magneto-optical Kerr rotations and ellipticities for all three materials. In the case of AuMnSn the largest, zero-temperature, polar Kerr rotation has been found to be -0.45° at about 1 eV photon energy. The computed MOKE spectra of AuMnSn are in qualitative agreement with recent experiments. The largest Kerr rotations of AuMnIn and AuMnSb have been calculated to be +0.64° at 4.3 eV and -0.85° at 0.9 eV, respectively.

Application of the post-source pulse-focusing technique in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: optimization of the experimental parameters and their influence on the capability of the method.

This paper describes experiments demonstrating the performance of a linear time-of-flight mass spectrometer equipped with the post-source pulse-focusing (PSPF) technique. The influence of various experimental parameters like the shape of the PSPF pulse on the performance of the instrument is discussed. The application of an ion lens in the acceleration region allows the focusing of high mass ions on the detector with a high yield. The observed mass resolution for matrix-assisted laser desorption/ionization (MALDI) generated ions is about 7000 (FWHM) and the mass accuracy using external standards for calibration is about 0.05% or better, in this work demonstrated for molecules with a mass up to 5700 Da. The percentage of the complete mass spectrum which can be detected with increased resolution and accuracy depends on the geometry of a particular setup. In order to cover a broad mass range several parameter sets have to be applied one after the other. Instead of the commonly employed microchannel plates, microsphere plates were used for detection of the ions in these experiments in order to test their applicability in combination with MALDI.

Protein conformational changes determined by matrix-assisted laser desorption mass spectrometry.

It is shown that simultaneously to the unfolding of hen egg white lysozyme and horse heart cytochrome c the sequential conformational changes and molten globule states can be detected by the combination of proteolysis and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). This is demonstrated by the differences among the products and the time courses of native lysozyme as well as those unfolded in 1 and 3 M guanidine hydrochloride (GuHCl) when they were proteolyzed by proteinase K and analyzed by MALDI-MS. Due to the absence of disulfide bonds in the cytochrome c molecule, it is more sensitive to the disturbance of the denaturant. The partially unfolded state as detected at low concentrations of guanidine hydrochloride in our experiment resemble the molten globule state. One of the unique properties of the method described herein is to measure directly the peptide fragment liberated from proteolysis of the protein. It allows the identification of the sensitive sites susceptible to denaturation, which are subsequently cleaved by proteinase K proteolysis.

Primary structures of proteins characterized by proteinase K digestion and matrix-assisted laser desorption/ionization mass spectrometry.

To improve the sequence ions of a protein in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), proteinase K was used to digest the protein followed by MALDI-MS characterization of the peptide fragments. The primary structures of three proteins, insulin B chain, cytochrome c and lysozyme, were determined by this method. A series of peptide fragments including those differentiated by one residue can be produced from the protein by using proteinase K digestion, thus providing support to the protein sequence. The peptide fragments liberated from proteinase K proteolysis of the insulin B chain allow the protein to be partially sequenced. Furthermore, some of the residues are double or triple checked by generating a variety of fragments. The same method was used to investigate cytochrome c and lysozyme denaturated in 3 M guanidine hydrochloride. The success of the method relies on the intrinsic properties of proteinase K and accurate determination of the peptide fragments by MALDI-MS.