Interplay of structural and electronic phase separation in single crystalline La(2)CuO(4.05) studied by neutron and Raman scattering

We report a neutron and Raman scattering study of a single-crystal of La(2)CuO(4.05) prepared by high temperature electrochemical oxidation. Elastic neutron scattering measurements show the presence of two phases, corresponding to the two edges of the first miscibility gap, all the way up to 300 K. An additional oxygen redistribution, driven by electronic energies, is identified at 250 K in Raman scattering (RS) experiments by the simultaneous onset of two-phonon and two-magnon scattering, which are fingerprints of the insulating phase. Elastic neutron scattering measurements show directly an antiferromagnetic ordering below a N\'eel temperature of T_N =210K. The opening of the superconducting gap manifests itself as a redistribution of electronic Raman scattering below the superconducting transition temperature, T_c = 24K. A pronounced temperature-dependent suppression of the intensity of the (100) magnetic Bragg peak has been detected below T_c. We ascribe this phenomenon to a change of relative volume fraction of superconducting and antiferromagnetic phases with decreasing temperature caused by a form of a superconducting proximity effect.Comment: 9 pages, including 9 eps figures, submitted to PR

Prophossi:automating expert validation of phosphopeptide-spectrum matches from tandem mass spectrometry

Motivation: Complex patterns of protein phosphorylation mediate many cellular processes. Tandem mass spectrometry (MS/MS) is a powerful tool for identifying these post-translational modifications. In high-throughput experiments, mass spectrometry database search engines, such as MASCOT provide a ranked list of peptide identifications based on hundreds of thousands of MS/MS spectra obtained in a mass spectrometry experiment. These search results are not in themselves sufficient for confident assignment of phosphorylation sites as identification of characteristic mass differences requires time-consuming manual assessment of the spectra by an experienced analyst. The time required for manual assessment has previously rendered high-throughput confident assignment of phosphorylation sites challenging