Irreversibility in quantum maps with decoherence

The Bolztmann echo (BE) is a measure of irreversibility and sensitivity to perturbations for non-isolated systems. Recently, different regimes of this quantity were described for chaotic systems. There is a perturbative regime where the BE decays with a rate given by the sum of a term depending on the accuracy with which the system is time-reversed and a term depending on the coupling between the system and the environment. In addition, a parameter independent regime, characterised by the classical Lyapunov exponent, is expected. In this paper we study the behaviour of the BE in hyperbolic maps that are in contact with different environments. We analyse the emergence of the different regimes and show that the behaviour of the decay rate of the BE is strongly dependent on the type of environment.Comment: 13 pages, 3 figures

Relaxation of isolated quantum systems beyond chaos

In classical statistical mechanics there is a clear correlation between relaxation to equilibrium and chaos. In contrast, for isolated quantum systems this relation is -- to say the least -- fuzzy. In this work we try to unveil the intricate relation between the relaxation process and the transition from integrability to chaos. We study the approach to equilibrium in two different many body quantum systems that can be parametrically tuned from regular to chaotic. We show that a universal relation between relaxation and delocalization of the initial state in the perturbed basis can be established regardless of the chaotic nature of system.Comment: 4+ pages, 4 figs. Closest to published versio

Rapid pre-gel visualization of proteins with mass spectrometry compatibility

Despite all of the prophecies of doom, gel electrophoresis is still prevalent in modern proteomic workflows. However, the currently used protein staining methods represent a serious bottleneck for a quick subsequent protein analysis using mass spectrometry. Substituting traditional protein stains by pre-gel derivatization with visible and mass spectrometry compatible reagents eliminates several processing steps and drastically reduces the sample preparation time. A defined chemistry permits seamless integration of such covalent protein staining methods into standardized bioinformatic pipelines. Using Uniblue A we could covalently stain simple to complex protein samples within 1 minute. Protein profiles on the gels were not compromised and MS/MS based sequence coverages higher than 80% could be obtained. In addition, the visual tracking of covalently stained proteins and peptides facilitates method development and validation. Altogether, this new chemo-proteomic approach enables true "at-line" analysis of proteins