Off shell behaviour of the in medium nucleon-nucleon cross section

The properties of nucleon-nucleon scattering inside dense nuclear matter are investigated. We use the relativistic Brueckner-Hartree-Fock model to determine on-shell and half off-shell in-medium transition amplitudes and cross sections. At finite densities the on-shell cross sections are generally suppressed. This reduction is, however, less pronounced than found in previous works. In the case that the outgoing momenta are allowed to be off energy shell the amplitudes show a strong variation with momentum. This description allows to determine in-medium cross sections beyond the quasi-particle approximation accounting thereby for the finite width which nucleons acquire in the dense nuclear medium. For reasonable choices of the in-medium nuclear spectral width, i.e. $\Gamma\leq 40$ MeV, the resulting total cross sections are, however, reduced by not more than about 25% compared to the on-shell values. Off-shell effect are generally more pronounced at large nuclear matter densities.Comment: 31 pages Revtex, 12 figures, typos corrected, to appear in Phys. Rev.

Microsecond folding of the cold shock protein measured by a pressure-jump technique

A pressure-jump apparatus was employed in investigating the kinetics of protein unfolding and refolding. In the reaction cell, the pressure can be increased or decreased by 100-160 bar within 50-100 mu s and then held constant. Thus, unfolding and refolding reactions in the time range from 70 mu s to 70 s can be followed with this technique. Measurements are possible in the transition regions of thermally or denaturant-induced folding in a wide range of temperatures and solvent conditions. We used this pressure-jump method to determine the temperature dependence of the rate constants of unfolding and refolding of the cold shock protein of Bacillus subtilis and of three variants thereof with Phe --> Ala substitutions in the central beta-sheet region. For all variants, the change in heat capacity occurred in refolding between the unfolded and activated states, suggesting that the overall native-like character of the activated state of folding was not changed by the deletion of individual Phe side chains. The Phe27Ala mutation affected the rate of unfolding only; the Phe15Ala and Phe17Ala mutations changed the kinetics of both unfolding and refolding. Although the activated state of folding of the cold shock protein is overall native-like, individual side chains are still in a non-native environment