A cylindrical liquid-core waveguide

A novel concept for a liquid-core lightguide in cylindrical symmetry is presented. For a concrete 17 cm long device using water as a core and the transparent fluorinated polymer Teflon as a cladding layer, the coupling efficiency and guiding properties are investigated theoretically and compared with experimental results. The guide is found to exhibit low losses. A possible application of this type of guide is investigated by replacing the optical cell of a standard UV/VIS spectrometer by the cylindrical liquid-core waveguide. An increasing sensitivity for especially low concentrations of a polluting dye by a factor of about 15 is observed. Concentrations as low as a few parts per billion of the pollutant can be detected with a good signal-to-noise ratio.     

A simple method for labelling proteins with211At via diazotized aromatic diamine

A simple and rapid method for labelling proteins with²¹¹At by means of a 1,4-diaminobenzene link is described. 1,4-diaminobenzene is transformed into the diazonium salt and subsequently reactions of both²¹¹At and proteins with the diazonium salt take place simultaneously. For possibly high yields of astatized protein an appropriate temperature of 273 K was found. The results demonstrate the difference between the reaction mechanisms of iodine and astatine with proteins.     

Hamiltonian structure of the nonlinear sigma model in light front coordinates

Theoretical and Mathematical Physics -     

The total hadronic cross section for e+e− annihilation between 3.1 and 4.8 GeV center of mass energy

Using the solenoidal magnetic detector PLUTO, we have measured the total cross section for e⁺e^? annihilation into hadrons. Results are presented for center of mass energies between 3.6 and 4.8 GeV, and in the regions of the $\text{J}\text{ψ}$(3.1) and ψ(3.7) resonances. We also present results for the 2 prong cross section in the energy range 3.6 to 4.8 GeV.     

Seven new hindered isomeric rhodopsins: A reexamination of the stereospecificity of the binding site of bovine opsin

Results of interaction of seven new geometric isomers of retinal (7-cis, 7,9-dicis; 7,11-dicis, 7,13-dicis; 9,11-dicis 7,9,11-tricis 7,9,13-tricis) with bovine opsin are reported. All of them form pigments with absorption maxima varying between 450 and 480 nm. The rates of pigment formation were generally considerably lower than those of 11-cis-retinal and the yields were less than quantitative. Implications of these results for the stereospecificity of the binding site of opsin are discussed.     

Whole cell matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and in situ structure analysis of streptocidins, a family of tyrocidine-like cyclic peptides

Streptocidins, a family of tyrocidine-like cyclic decapeptides, are an ideal demonstration object for the detection and in situ structure analysis of natural compounds directly in microbial cells using whole cell matrix-assisted laser desorption/ionization time-of-flight-mass spectrometry (MALDI-TOFMS), an emerging technique that can be used for rapid sensitive metabolic profiling of microorganisms. Five main members of the streptocidin family (A-E) were detected in Brevibacillus cells picked from agar plates and identified by in situ structure analysis with post-source decay MALDI-TOFMS. This efficient modern method allows the precise detection of metabolites within minutes without the need to isolate and purify the target compounds. The generated mass spectra are of similar quality to those obtained for the purified peptides. In addition, surface extracts were prepared by treating Brevibacillus cells with 70% acetonitrile in the presence of 0.1% trifluoroacetic acid and fractionated by high-resolution reversed-phase high-performance liquid chromatography (HPLC). In this way ten minor streptocidins were detected demonstrating the full biosynthetic variety of streptocidin production on the cellular level. The streptocidins differ from the well-known tyrocidines essentially in position 3 of the decapeptide chain by replacement of the aromatic amino acid (F/W) found in tyrocidines by L-leucine or L-valine.