Tensor product Gauss-Lobatto points are Fekete points for the cube

Tensor products of Gauss-Lobatto quadrature points are frequently used as collocation points in spectral element methods. Unfortunately, it is not known if Gauss-Lobatto points exist in non-tensor-product domains like the simplex. In this work, we show that the -dimensional tensor-product of Gauss-Lobatto quadrature points are also Fekete points. This suggests a way to generalize spectral methods based on Gauss-Lobatto points to non-tensor-product domains, since Fekete points are known to exist and have been computed in the triangle and tetrahedron. In one dimension this result was proved by Fejér in 1932, but the extension to higher dimensions in non-trivial.

     

The osmotic pressure of 3He-4He mixtures along the phase separation curve

The osmotic pressure of ³He-⁴He mixtures was measured along the phase separation curve at temperatures up to 500 mK by balancing it with the fountain pressure of pure ⁴He. The usefullness of the secondary osmotic pressure thermometer was reinvestigated.     

Photocycloaddition reactions of the first stable thioaldehyde: 2,4,6-tri(tert-butyl)thiobenzaldehyde with substituted allenes

Irradiation of 2,4,6-tri-(tert,-butyl)thiobenzaldehyde $\text{1}$ with some alkoxy-, alkylthio-, and phenyl-allenes $\text{2}$$\text{a}$-$\text{i}$ gave one stereoisomer of a (2+2)-cycloadduct, viz. thietane $\text{3}$ in high yields (75–95%). Ringclosure is in agreement with MNDO-calculations.     

Fürj≦n—3 sind zweij-Zellen desR n stets verbindbar

Ohne Zusammenfassung     

Book reviews

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Book reviews

     

Evidence against the S-meson

Measurements are reported of p?p total cross sections from 388 to 599 MeV/c in small momentum steps. Statistical errors are typically ±0.4%and the normalisation uncertainty is ±0.7%. There is no evidence for the “S-meson”.     

Study on the aggregation of teicoplanin

The aggregation of teicoplanin was studied in four solutions: 0.06 M phosphate buffers pH 4.3 and 6.3, both with and without 10% (v/v) of acetonitrile. Conductometry, capillary electrophoresis, cyclic voltammetry, and static light scattering were employed to determine the critical micelle concentration (CMC) of teicoplanin. Dynamic light scattering was used to give an additional information on the size and the size distribution of the particles formed. While the CMC was found in solutions without acetonitrile, attempts to detect any CMC failed in solutions containing acetonitrile. The results point out to different solvating mechanism in solutions with and without acetonitrile, leading to two different schemes of association.     

Characterization of cyclofructan-based chiral stationary phases by linear free energy relationship

Cyclofructans (CFs), a new class of chiral selectors, have been recently introduced for application in liquid chromatography and capillary electrophoresis. So far, derivatized CFs have performed interesting separation possibilities for a variety of compounds. The current work is focused on characterization of three different CF-based chiral stationary phases (CF-based CSPs), i.e. isopropyl carbamate cyclofructan 6 (IP-CF6), R-naphthylethyl carbamate cyclofructan 6 (RN-CF6) and dimethylphenyl carbamate cyclofructan 7 (DMP-CF7). The linear free energy relationship (LFER) model was used to reveal the dominant interactions participating in the complex retention mechanism. A set of 44 different test solutes, with known solvation parameters, was used to determine the regression coefficients of the LFER equation under two mobile-phase compositions in normal separation mode. The LFER results showed that hydrogen bond acidity, hydrophobicity and dipolarity/polarizibility mostly affect the retention and separation process on the CF-based columns in the studied separation systems.     

Cyclofructan 6 based stationary phases for hydrophilic interaction liquid chromatography

New stationary phases for hydrophilic interaction liquid chromatography (HILIC) were synthesized by covalently attaching native cyclofructan 6 (CF6) to silica gel. The chromatographic characteristics of the new stationary phases were evaluated and compared to three different types of commercial HILIC columns. The CF6 columns produced considerably different retention and selectivity patterns for various classes of polar analytes, including nucleic acid compounds, xanthines, β-blockers, salicylic acid and its derivatives, and maltooligosaccharides. Univariate optimization approaches were examined including organic modifier (acetonitrile) contents and buffer pH and salt concentration. The thermodynamic characteristic of the CF6 stationary phase was investigated by considering the column temperature effect on retention and utilizing van't Hoff plots. CF6 based stationary phases appear to have exceptionally broad applicability for HILIC mode separations.     

Solid-state NMR on a large multidomain integral membrane protein: the outer membrane protein assembly factor BamA

Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and intrinsic flexibility. We show here that motional-filtered high-resolution solid-state NMR (ssNMR) experiments allow for the observation and structural analysis of very large multidomain membrane proteins that are characterized by different motional time scales. This approach was used to probe the folding of the 790-residue membrane protein BamA, which is the core component of the Escherichia coli outer membrane protein assembly machinery. A combination of dipolar- and scalar-based two-dimensional ssNMR experiments applied to two uniformly (13)C,(15)N-labeled BamA variants revealed characteristic secondary structure elements and distinct dynamics within the BamA transmembrane protein segment and the periplasmic POTRA domains. This approach hence provides a general strategy for collecting atomic-scale structural information on multidomain (membrane) proteins in a native-like environment.