Measurement of gamma p --> K+ Lambda and gamma p --> K+ Sigma0 at photon energies up to 2.6 GeV

The reactions gamma p --> K+ Lambda and gamma p --> K+ Sigma0 were measured in the energy range from threshold up to a photon energy of 2.6 GeV. The data were taken with the SAPHIR detector at the electron stretcher facility, ELSA. Results on cross sections and hyperon polarizations are presented as a function of kaon production angle and photon energy. The total cross section for Lambda production rises steeply with energy close to threshold, whereas the Sigma0 cross section rises slowly to a maximum at about E_gamma = 1.45 GeV. Cross sections together with their angular decompositions into Legendre polynomials suggest contributions from resonance production for both reactions. In general, the induced polarization of Lambda has negative values in the kaon forward direction and positive values in the backward direction. The magnitude varies with energy. The polarization of Sigma0 follows a similar angular and energy dependence as that of Lambda, but with opposite sign.Comment: 21 pages, 25 figures, submitted to Eur. Phys. J.

Evidence for the positive-strangeness pentaquark Θ+\Theta^+ in photoproduction with the SAPHIR detector at ELSA

The positive--strangeness baryon resonance $\Theta^+$ is observed in photoproduction of the $\rm nK^+K^0_s$ final state with the SAPHIR detector at the Bonn ELectron Stretcher Accelerator ELSA. It is seen as a peak in the $\rm nK^+$ invariant mass distribution with a $4.8\sigma$ confidence level. We find a mass $\rm M_{\Theta^+} = 1540\pm 4\pm 2$ MeV and an upper limit of the width $\rm \Gamma_{\Theta^+} < 25$ MeV at 90% c.l. From the absence of a signal in the $\rm pK^+$ invariant mass distribution in $\rm\gamma p\to pK^+K^-$ at the expected strength we conclude that the $\Theta^+$ must be isoscalar.Comment: 9 pages, 4 figure

K0-Sigma+ Photoproduction with SAPHIR

Preliminary results of the analysis of the reaction p(gamma,K0)Sigma+ are presented. We show the first measurement of the differential cross section and much improved data for the total cross section than previous data. The data are compared with model predictions from different isobar and quark models that give a good description of p(gamma,K+)Lambda and p(gamma,K+)Sigma0 data in the same energy range. Results of ChPT describe the data adequately at threshold while isobar models that include hadronic form factors reproduce the data at intermediate energies.Comment: 4 pages, Latex2e, 4 postscript figures. Talk given at the International Conference on Hypernuclear and Strange Particle Physics (HYP97), Brookhaven National Laboratory, USA, October 13-18, 1997. To be published in Nucl. Phys. A. Revised version due to changes in experimental dat

Drift chamber with a c-shaped frame

We present the construction of a planar drift chamber with wires stretched between two arms of a c-shaped aluminium frame. The special shape of the frame allows to extendthe momentum acceptance of the COSY-11 detection system towards lower momenta without suppressing the high momentum particles. The proposed design allows for construction of tracking detectors covering small angles with respect to the beam, which can be installed and removed without dismounting the beam-pipe. For a three-dimensional track reconstruction a computer code was developed using a simple algorithm of hit preselection.Comment: submitted to Nucl. Instr. & Meth

Contamination of Chalk groundwater by chlorinated solvents : a case study of deep penetration by non-aqueous phase liquids

The transport behaviour of chlorinated solvents, both in the aqueous phase and as a dense non-aqueous phase liquid (DNAPL), in fissured microporous aquifers is reviewed. The presence of DNAPL in aquifers is especially serious as it is likely to be the main subsurface source of contamination and, given the slow rates of dissolution in groundwater, may persist for decades. However, the identification and quantification of DNAPLs in fractured aquifers present many practical problems and are often not achievable. A case study of a Chalk site which had been contaminated by chlorinated solvents demonstrated that the use of a range of techniques, including depth profiling of solvent porewater concentrations in cored boreholes, can provide clear evidence for the presence of DNAPL at depth, although DNAPL was not itself observed. Theoretical considerations and field observations confirmed that DNAPL movement is via fractures rather than through the microporous matrix

天下第一楼（剧本）

The photoproduction of the vector meson $\omega$ has been studied between threshold and W = 2.4 GeV with the SAPHIR detector at the Bonn electron stretcher ring ELSA. Besides, the total cross-sections angular distributions in the CMS and decay angular distributions in the helicity and Gottfried-Jackson systems have been measured

Bayesian Model Selection Applied to the Analysis of Fluorescence Correlation Spectroscopy Data of Fluorescent Proteins in Vitro and in Vivo

Fluorescence correlation spectroscopy (FCS) is a powerful technique to investigate molecular dynamics with single molecule sensitivity. In particular, in the life sciences it has found widespread application using fluorescent proteins as molecularly specific labels. However, FCS data analysis and interpretation using fluorescent proteins remains challenging due to typically low signal-to-noise ratio of FCS data and correlated noise in autocorrelated data sets. As a result, naive fitting procedures that ignore these important issues typically provide similarly good fits for multiple competing models without clear distinction of which model is preferred given the signal-to-noise ratio present in the data. Recently, we introduced a Bayesian model selection procedure to overcome this issue with FCS data analysis. The method accounts for the highly correlated noise that is present in FCS data sets and additionally penalizes model complexity to prevent over interpretation of FCS data. Here, we apply this procedure to evaluate FCS data from fluorescent proteins assayed in vitro and in vivo. Consistent with previous work, we demonstrate that model selection is strongly dependent on the signal-to-noise ratio of the measurement, namely, excitation intensity and measurement time, and is sensitive to saturation artifacts. Under fixed, low intensity excitation conditions, physical transport models can unambiguously be identified. However, at excitation intensities that are considered moderate in many studies, unwanted artifacts are introduced that result in nonphysical models to be preferred. We also determined the appropriate fitting models of a GFP tagged secreted signaling protein, Wnt3, in live zebrafish embryos, which is necessary for the investigation of Wnt3 expression and secretion in development. Bayes model selection therefore provides a robust procedure to determine appropriate transport and photophysical models for fluorescent proteins when appropriate models are provided, to help detect and eliminate experimental artifacts in solution, cells, and in living organisms.National Science Foundation (U.S.). Physics of Living Systems ProgramNational Institute of Mental Health (U.S.) (Award U01MH106011

Dysferlin Forms a Dimer Mediated by the C2 Domains and the Transmembrane Domain In Vitro and in Living Cells

Dysferlin was previously identified as a key player in muscle membrane repair and its deficiency leads to the development of muscular dystrophy and cardiomyopathy. However, little is known about the oligomerization of this protein in the plasma membrane. Here we report for the first time that dysferlin forms a dimer in vitro and in living adult skeletal muscle fibers isolated from mice. Endogenous dysferlin from rabbit skeletal muscle exists primarily as a ∼460 kDa species in detergent-solubilized muscle homogenate, as shown by sucrose gradient fractionation, gel filtration and cross-linking assays. Fluorescent protein (YFP) labeled human dysferlin forms a dimer in vitro, as demonstrated by fluorescence correlation spectroscopy (FCS) and photon counting histogram (PCH) analyses. Dysferlin also dimerizes in living cells, as probed by fluorescence resonance energy transfer (FRET). Domain mapping FRET experiments showed that dysferlin dimerization is mediated by its transmembrane domain and by multiple C2 domains. However, C2A did not significantly contribute to dimerization; notably, this is the only C2 domain in dysferlin known to engage in a Ca-dependent interaction with cell membranes. Taken together, the data suggest that Ca-insensitive C2 domains mediate high affinity self-association of dysferlin in a parallel homodimer, leaving the Ca-sensitive C2A domain free to interact with membranes

Fluorescence Polarization and Fluctuation Analysis Monitors Subunit Proximity, Stoichiometry, and Protein Complex Hydrodynamics

Förster resonance energy transfer (FRET) microscopy is frequently used to study protein interactions and conformational changes in living cells. The utility of FRET is limited by false positive and negative signals. To overcome these limitations we have developed Fluorescence Polarization and Fluctuation Analysis (FPFA), a hybrid single-molecule based method combining time-resolved fluorescence anisotropy (homo-FRET) and fluorescence correlation spectroscopy. Using FPFA, homo-FRET (a 1–10 nm proximity gauge), brightness (a measure of the number of fluorescent subunits in a complex), and correlation time (an attribute sensitive to the mass and shape of a protein complex) can be simultaneously measured. These measurements together rigorously constrain the interpretation of FRET signals. Venus based control-constructs were used to validate FPFA. The utility of FPFA was demonstrated by measuring in living cells the number of subunits in the α-isoform of Venus-tagged calcium-calmodulin dependent protein kinase-II (CaMKIIα) holoenzyme. Brightness analysis revealed that the holoenzyme has, on average, 11.9±1.2 subunit, but values ranged from 10–14 in individual cells. Homo-FRET analysis simultaneously detected that catalytic domains were arranged as dimers in the dodecameric holoenzyme, and this paired organization was confirmed by quantitative hetero-FRET analysis. In freshly prepared cell homogenates FPFA detected only 10.2±1.3 subunits in the holoenzyme with values ranging from 9–12. Despite the reduction in subunit number, catalytic domains were still arranged as pairs in homogenates. Thus, FPFA suggests that while the absolute number of subunits in an auto-inhibited holoenzyme might vary from cell to cell, the organization of catalytic domains into pairs is preserved