Search for exotic mesons at SLAC
The theoretical justification and results from recent experimental searches for backward-produced exotic mesons including two experiments carried out by the collaboration at SLAC are reviewed. The first experiment put upper limits of about 1 to 2 $mu$b for X$sup ++$ $Yields$ (2$pi$, 4$pi$, 6$pi$)$sup ++$ and anti pp$pi$$sup +$$pi$$sup +$ in the reaction $pi$$sup +$ + p $Yields$ X$sup ++$ + n/sub forward/ at 8.4 GeV/c studied with the SLAC 14 inch rapid cycling bubble chamber triggered by a downstream neutron detector. Also the important features of the recently completed second experiment with the SLAC streamer chamber to study the reaction $pi$$sup -$ + p $Yields$ X$sup --$ + p/sub forward/ at 14 GeV/c are discussed. (auth)
Search for exotics produced opposite a forward Λ in 15 GeV/c π+p interactions
We have carried out a search for exotic meson resonances produced in the reaction π+p→K++ + Λ (forward) at 15 GeV/c. We have found no evidence for the existence of resonance-like states in the K++ system, and have obtained 95% confidence level upper limits of 1.7 μb on their production with masses <2.8 GeV, and 2.6 μb with masses between 2.8 GeV and 4 GeV.
Collagen dynamics in articular cartilage under osmotic pressure
Cartilage is a complex biological tissue consisting of collagen, proteoglycans and water. The structure and molecular mobility of the collagen component of cartilage were studied by 13C solid‐state NMR spectroscopy as a function of hydration. The hydration level of cartilage was adjusted between fully hydrated (∼80 wt% H2O) and highly dehydrated (∼30 wt% H2O) using the osmotic stress technique. Thus, the conditions of mechanical load could be simulated and the response of the tissue macromolecules to mechanical stress is reported. From the NMR measurements, the following results were obtained. (i) Measurements of motionally averaged dipolar 1H–13C couplings were carried out to study the segmental mobility in cartilage collagen at full hydration. Backbone segments undergo fast motions with amplitudes of ∼35° whereas the collagen side‐chains are somewhat more mobile with amplitudes between 40 and 50°. In spite of the high water content of cartilage, collagen remains essentially rigid. (ii) No chemical shift changes were observed in 13C cross‐polarization magic angle spinning spectra of cartilage tissue at varying hydration indicating that the collagen structure was not altered by application of high osmotic stress. (iii) The 1H–13C dipolar coupling values detected for collagen signals respond to dehydration. The dipolar coupling values gradually increase upon cartilage dehydration, reaching rigid limit values at ∼30 wt% H2O. This indicates that collagen is essentially dehydrated in cartilage tissue under very high mechanical load, which provides insights into the elastic properties of cartilage collagen, although the mechanical pressures applied here exceed the physiological limit. Copyright © 2006 John Wiley & Sons, Ltd.