The Stability and Formation of Native Proteins from Unfolded Monomers Is Increased through Interactions with Unrelated Proteins

The intracellular concentration of protein may be as high as 400 mg per ml; thus it seems inevitable that within the cell, numerous protein-protein contacts are constantly occurring. A basic biochemical principle states that the equilibrium of an association reaction can be shifted by ligand binding. This indicates that if within the cell many protein-protein interactions are indeed taking place, some fundamental characteristics of proteins would necessarily differ from those observed in traditional biochemical systems. Accordingly, we measured the effect of eight different proteins on the formation of homodimeric triosephosphate isomerase from Trypanosoma brucei (TbTIM) from guanidinium chloride unfolded monomers. The eight proteins at concentrations of micrograms per ml induced an important increase on active dimer formation. Studies on the mechanism of this phenomenon showed that the proteins stabilize the dimeric structure of TbTIM, and that this is the driving force that promotes the formation of active dimers. Similar data were obtained with TIM from three other species. The heat changes that occur when TbTIM is mixed with lysozyme were determined by isothermal titration calorimetry; the results provided direct evidence of the weak interaction between apparently unrelated proteins. The data, therefore, are strongly suggestive that the numerous protein-protein interactions that occur in the intracellular space are an additional control factor in the formation and stability of proteins

Measurement of the relative width difference of the B0B^0-Bˉ0\bar B^0 system with the ATLAS detector

20 pages plus author list + cover page (38 pages total), 5 figures, 2 tables, submitted to Journal of High Energy Physics, All figures including auxiliary figures are available at http://atlas.web.cern.ch/Atlas/GROUPS/PHYSICS/PAPERS/BPHY-2015-01/ - See paper for full list of authorsInternational audienceThis paper presents the measurement of the relative width difference $\Delta \Gamma_d / \Gamma_d$ of the $B^0$-$\bar B^0$ system using the data collected by the ATLAS experiment at the LHC in $p p$ collisions at $\sqrt{s} = 7$ TeV and $\sqrt{s} = 8$ TeV and corresponding to an integrated luminosity of 25.2 fb$^{-1}$. The value of $\Delta \Gamma_d / \Gamma_d$ is obtained by comparing the decay-time distributions of $B^0 \to J/\psi K_S$ and $B^0 \to J/\psi K^{*0}(892)$ decays. The result is \Delta \Gamma_d / \Gamma_d = (-0.1 \pm 1.1~\mbox{(stat.)} \pm 0.9~\mbox{(syst.)}) \times 10^{-2}. Currently, this is the most precise single measurement of $\Delta \Gamma_d / \Gamma_d$. It agrees with the Standard Model prediction and the measurements by other experiments

La formazione delle parole nei linguaggi di specializzazione in tedesco: una prospettiva didattica per il lessico medico

In this paper some typical features of word-formation processes in scientific German are analyzed in a didactic perspective, with particular attention to medical language. In the introductory part I briefly discuss some general aspects of teaching languages for special purposes and I underline the importance of the grammatical reflection on word-formation in LSP, in particular when dealing with a language having a very transparent terminology such as the medical one. In the main part I analyse the most relevant handbooks of German medical language and I suggest methodological approaches to medical vocabulary teaching to Italian students. Particular importance is thereby given to the setting of terminology in authentic text