Structural and thermal study of calcium undecanoate

In the present work, an X-ray diffraction (XRD) and thermal study of calcium undecanoate is presented. The measured high-resolution XRD powder pattern of the synthesized salt at room temperature, using synchrotron radiation, showed that the salt is a mixture of monohydrated and anhydrous calcium undecanoate. Calcium undecanoate monohydrate proved to have a monoclinic cell with a symmetry described by the P2₁/a space group. The structure dehydrates at about 100°C. After dehydration, the salt undergoes a phase transformation which results in a thermotropic mesophase. Further heating of the salt leads to decomposition and melting. Ketones are the probable products of decomposition at 400°C.     

Measurement of the total and differential cross sections for the reaction π − p → ηn with the Crystal Ball detector

The first results obtained in 1998 by the Crystal Ball collaboration from a measurement of the total and differential cross sections for the reaction π ^? p → ηn are presented. These new experimental results for the total cross sections are compared with the predictions of the K-matrix model for pion-nucleon scattering. The angular distribution at momenta near the reaction threshold (685 MeV/c) is determined by the S-wave contribution. The P-wave contribution begins to manifest itself from a momentum of 720 MeV/c.     

On self-similar solutions of semilinear wave equations in higher space dimensions

In this paper we analyze self-similar solutions of the semilinear wave equation Φ_tt − ΔΦ − Φ^p = 0 for n > 3 space dimensions. We found several classes of analytic solutions labeled by a single parameter, the form of which differ in the vicinity of the light cone. We also propose suitable numerical methods to study them.     

Characterization of a cross-linked DNA-Endonuclease VIII repair complex by electrospray ionization mass spectrometry

Electrospray mass spectrometry techniques were used to characterize components of the active site in Endonuclease VIII by identifying the amino acid sequence and the binding site for a tryptic peptide derived from Endo VIII in a cross-linked DNA-peptide complex. Endo VIII, a DNA repair enzyme with both glycosylase and lyase activities, was covalently bound to a thymidine glycol-containing oligodeoxynucleotide duplex by converting a transient Schiff base formed during the course of the glycosylase activity to a stable covalent bond by chemical reduction with sodium borohydride. After tryptic digestion of the initial product, the identification of the cross-linked peptide was deduced initially from the molecular mass of the tryptic product obtained by negative ion electrospray mass analysis. Nanospray tandem mass spectrometry (MS/MS) analysis of the tryptic product corroborated the molecular mass of the peptide fragment and verified the point of attachment to the oligomer, but failed to produce sufficient fragmentation to sequence the peptide completely. Direct evidence for the amino acid sequence of the peptide was obtained after enzymatic digestion of the DNA portion of the cross-linked DNA-peptide product and analysis by negative ion nanospray MS/MS. Examination of the ions from collision induced fragmentation disclosed that this substance was the N-terminal tryptic fragment of Endo VIII cross-linked to a portion of the oligomer, and that the N-terminal proline from Endo VIII was covalently bound to the residual deoxyribose moiety at the original location of the thymine glycol in the oligomer.