Mg-promoted facile and selective intramolecular cyclization of aromatic δ-ketoesters

Treatment of various types of aromatic δ-ketoesters 2, 7, and 9 with Mg-turnings for Grignard reaction at −5 to 0 °C in N,N-dimethylformamide (DMF) containing trimethylsilyl chloride (TMSCl) brought about selective and reductive intramolecular cyclization to give the corresponding α-aryl-α-hydroxycyclopentanones 5, 8, and 10, respectively, in moderate to good yields. Similar reductive intramolecular cyclization of aromatic δ-ketodiesters 14, followed by acidic hydrolysis and decarboxylation easily gave the corresponding 2-aryl-2-cyclopenten-1-ones 15. The present facile coupling may be initiated through electron transfer from Mg metal to the aromatic carbonyl groups of 2, 7, 9, and 14 to generate the corresponding radical anions, followed by their intramolecular nucleophilic attack to the ester groups to give the corresponding five-membered ring compounds 5, 8, 10, and 15, respectively.     

Protective effect of small amounts of sodium dodecyl sulfate on the helical structure of bovine serum albumin in thermal denaturation

In the presence of sodium dodecyl sulfate (SDS), the secondary structure of bovine serum albumin (BSA) was almost protected against thermal denaturation above 50 degrees C, where the structural change became irreversible. Beyond 30 degrees C, the helicity (66%) of the protein sharply decreased with rise of temperature. In response to this, the proportions of beta-structure and random coil increased. The helicity and the beta-structural proportion were 44% and 13% at 65 degrees C, respectively. The protective effect was observed upon the coexistence of SDS of extremely low concentrations: the molar ratio of [SDS]/[BSA] of 15 was enough to induce the maximal protective effect on the helical structure of the protein. The maximal protected helicity was 58% at 65 degrees C, increasing to 64% upon cooling down to 25 degrees C. This protective effect became greater with an increase of chain length of alkyl sulfate ion. On the other hand, a cationic surfactant did not protect the BSA structure at all against the thermal denaturation. This protective effect was characterized by the specific amphiphilic nature of anionic surfactant. Such an anionic surfactant is considered to protect the protein structure by building bridges between particular nonpolar residues and particular positively charged residues located on different loops of the protein.     

A new N~* resonance as a hadronic molecular state

We report our recent work on a hadronic molecule state of the K(K)N system with I=1/2 and J~P=1/2~+. We assume that the A(1405) resonance and the scalar mesons, f_0(980), a_0(980), are reproduced as quasi-bound states of (K)N and K(K), respectively. Performing non-relativistic three-body calculations with a variational method for this system, we find a quasibound state of the K(K)N system around 1910 MeV below the three-body breakup threshold. This state corresponds to a new baryon resonance of N~* with J~P = 1/2~+. We find also that this resonance has the cluster structure of the two-body bound states keeping their properties as in the isolated two-particle systems. We also briefly discuss another hadronic molecular state composed by two (K) and one (N), which corresponds to a Ξ~* resonance.     

Baryon resonances as hadronic molecule states with kaons

We investigate hadronic molecule states of $K \bar K N$ and $\bar K \bar K N$ systems with I?=?1/2 and J ^P ?=?1/2^?+?, assuming that Λ(1405) and the scalar mesons, f ₀(980), a ₀(980), are reproduced as quasi-bound states of $\bar KN$ and $K \bar K$ . Performing non-relativistic three-body calculations for these systems, we find weakly bound states for $K \bar K N$ and $\bar K \bar K N$ around 1900 MeV, which correspond to new baryon resonances of N ^* and Ξ ^* with J ^P ?=?1/2^?+?. We find that these resonances have cluster structure of the two-body bound state keeping its properties as in the isolated two-particle system.     

Listeria monocytogenes cells injured by high hydrostatic pressure and their recovery in nutrient-rich or -free medium during cold storage

ABSTRACT

Cells of Listeria monocytogenes suspended in phosphate-buffered saline (PBS) were treated by high hydrostatic pressure (HHP; 500?MPa, 25°C, 10?min), diluted by ten folds using trypticase soy broth (TSB) or PBS, and stored at cold temperatures of 0–15°C. Viable cell count in TSB increased logarithmically close to the initial count at each storage temperature, while that in PBS increased temporarily and subsequently decreased to almost nondetectable level except the case at 15°C, where it showed logarithmic increase thereafter. Based on proliferation experiments where their healthy cells were inoculated to TSB or to PBS containing their heat-killed dead cells, it was suggested that increase in the viable count of HHP-treated cells in TSB and PBS could be ascribed to the recovery of colony forming ability and/or proliferation depending on the cold storage temperature.     

Vibrational spectrum and specific heat of fine particles

The vibrational spectrum for a fine particle is obtained by exactly solving the wave equation for a homogeneous elastic sphere with free surface. In terms of this frequency spectrum, enhancements in the specific heat of fine particles are calculated and compared with the experiments at low temperatures. Qualitative features of the experimental results are consistently explained in our theory.     

Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 to 130°c

Silk fibroin films in the random-coil and β-form conformations were immersed in water at temperatures from 2 to 130°C, and conformational changes were followed by x-ray diffraction, infrared spectroscopy and differential scanning calorimetry. On treatment with water below 60°C, the random-coil conformation is converted to the α form and above 70°C to mixtures of the α and β conformations. The β-form content increases as the immersion temperature is raised. The β form is not affected by immersion in water in the temperature range studied.