Classical Hadrodynamics: A New Approach to Ultrarelativistic Heavy-Ion Collisions

We discuss a new approach to ultrarelativistic heavy-ion collisions based on classical hadrodynamics for extended nucleons, corresponding to nucleons of finite size interacting with massive meson fields. This new theory provides a natural covariant microscopic approach that includes automatically spacetime nonlocality and retardation, nonequilibrium phenomena, interactions among all nucleons and particle production. In the current version of our theory, we consider $N$ extended unexcited nucleons interacting with massive neutral scalar ($\sigma$) and neutral vector ($\omega$) meson fields. The resulting classical relativistic many-body equations of motion are solved numerically without further approximation for soft nucleon-nucleon collisions at $p_{\rm lab}$ = 14.6, 30, 60, 100 and 200 GeV/$c$ to yield the transverse momentum imparted to the nucleons. For the future development of the theory, the isovector pseudoscalar ($\pi^+$, $\pi^-$, $\pi^0$), isovector scalar ($\delta^+$, $\delta^-$, $\delta^0$), isovector vector ($\rho^+$, $\rho^-$, $\rho^0$) and neutral pseudoscalar ($\eta$) meson fields that are known to be important from nucleon-nucleon scattering experiments should be incorporated. In addition, the effects of quantum uncertainty on the equations of motion should be included by use of techniques analogous to those used by Moniz and Sharp for nonrelativistic quantum electrodynamics.Comment: 6 pages, LA-UR-94-217

FOTE 2008 Conference Report

A report prepared by JA.Net and ULCC about the Future of Technology in Education (FOTE 2008) conference, Imperial College, 3rd October 2008. It covers the main speakers, themes and presentations: Cloud Computing, Second Life, Portability, Personalisation, Shared Services, Campus of the Future, Mobile Technology, Creativity and Media Production, Social Collaboration Tools for Staff and Students

Tunnel-diode circuit features zero-level clipping

Tunnel-diode circuit starts clipping action as input voltage crosses zero axis. This clipper circuit is effective as limiter in FM receiver

A continuous physiological data collector

COP-DAC system utilizes oxygen and carbon dioxide analyzers, gas-flow meter, gas breathe-through system, analog computer, and data storage system to provide actual rather than average measurements of physiological and metabolic functions

CMS Product Sheet

Product sheet describing ULCC's Hosted Content Management Systems (CMS

A Global Survey of Community Reinvestment Laws: The Obligation of the Private Sector to Serve the Underserved in Several Countries

Summaries of the community reinvestment legislation in the United States, United Kingdom, Nigeria, Brazil, South Africa, India, Australia, and Canada

The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation.

Ssa1/2p, members of one of the yeast cytosolic hsp70 subfamilies, have been implicated in the translocation of secretory proteins into the lumen of the ER. The involvement of these hsp70s in translocation was tested directly by examining the effect of immunodepleting Ssa1/2p from yeast cytosol and subsequently testing the cytosol for its ability to support co- and post-translational translocation of prepro-alpha-factor. Depletion of Ssa1/2p had no effect on the efficiency of translocation in this in vitro assay. The system was used to examine the effect of the absence of Ssa1/2p on two other putative hsp70 functions: cotranslational folding of nascent luciferase and refolding of denatured luciferase. Depletion of Ssa1/2p had no effect on the ability of the yeast lysate to synthesize enzymatically active luciferase, but had a dramatic effect on the ability of the lysate to refold chemically denatured luciferase. These results demonstrate, for the first time, the refolding activity of Ssa1/2p in the context of the yeast cytosol, and define refolding activity as a chaperone function specific to Ssa1/2p, aprt from other cytosolic hsp70s. They also suggest that Ssa1/2p do not play a significant role in chaperoning the folding of nascent polypeptides. The implications of these findings for Ssa1/2p activity on their proposed role in the process of translocation are discussed