Quantification of specific proteins depends on separation by chromatography or electrophoresis followed by chemical detection schemes such as staining and fluorophore adhesion. Chemical exchange of short-lived isotopes, particularly sulfur, is also prevalent despite the inconveniences of counting radioactivity. Physical methods based on isotopic and elemental analyses offer highly sensitive protein quantitation that has linear response over wide dynamic ranges and is independent of protein conformation. Accelerator mass spectrometry quantifies long-lived isotopes such as 14C to sub-attomole sensitivity. We quantified protein interactions with small molecules such as toxins, vitamins, and natural biochemicals at precisions of 1-5% . Micro-proton-induced-xray-emission quantifies elemental abundances in separated metalloprotein samples to nanogram amounts and is capable of quantifying phosphorylated loci in gels. Accelerator-based quantitation is a possible tool for quantifying the genome translation into proteome.

The radiation pressure coupling with vacuum fluctuations gives rise to energy damping and decoherence of an oscillating particle. Both effects result from the emission of pairs of photons, a quantum effect related to the fluctuations of the Casimir force. We discuss different alternative methods for the computation of the decoherence time scale. We take the example of a spherical perfectly-reflecting particle, and consider the zero and high temperature limits. We also present short general reviews on decoherence and dynamical Casimir effect.

This article discusses an analysis of ultraviolet observations with the FAUST shuttle-borne telescope toward the Antennae and NGC 6752 celestial regions resulting in the detection of 46 and 221 candidate sources respectively, for a signal-to-noise ratio of 8.