HBT with space- vs. time-like hydrodynamic freeze-out

Bose-Einstein correlations in relativistic heavy ion collisions and their dependence on the freeze-out condition in hydrodynamic models is examined. The Cooper & Fryespace-like freeze-out mechanism is compared totime-like freeze-out, where particles are emittedaway only from the surface, i.e. space- vs. time-like freeze-out. The corresponding HBT radii are calculated for the two models emphasizing the difference in the outward HBT radius.     

Bose-Einstein correlations in thermal field theory

Two-particle correlation functions are calculated for bosons emitted from a localized thermal source (the “glow” of a “hot spot”). In contrast to existing work, non-equilibrium effects up to first order in gradients of the particle distribution function are taken into account. The spectral width of the bosons is shown to be an important quantity: if it is too small, they do not equilibrate locally and therefore strongly increase the measured correlation radius.     

Modification of transmembrane and GPI-anchored proteins on living cells by efficient protein trans-splicing using the Npu DnaE intein

The naturally split Npu DnaE intein can be used for ligation of an exogenous polypeptide to membrane proteins on living cells. No reducing agents or other factors are required. The approach is rapid and virtually traceless, because the intein removes itself during the reaction.     

Expanded Click Conjugation of Recombinant Proteins with Ubiquitin-Like Modifiers Reveals Altered Substrate Preference of SUMO2-Modified Ubc9

Wrestling with SUMO: The chemical conjugation of proteins with small ubiquitin-like modifiers (SUMO) can be achieved by a copper(I)-catalyzed cycloaddition and unnatural amino acid mutagenesis. This approach overcomes previous restrictions related to the primary sequence of proteins and coupling conditions. Moreover, biochemical data suggests that this triazole linkage presents the modifier in a proper distance and orientation relative to the target protein.     

Combination of acid labile detergent and C18 Empore™ disks for improved identification and sequence coverage of in-gel digested proteins

A protocol for improved extraction of peptides from in-gel protein digests, using a combination of the acid labile surfactant, sodium deoxycholate (SDC) and C18 Empore™ membranes, is presented. This approach results in better mass spectrum quality, higher numbers of identified peptide peaks and improved identification scores compared to standard tryptic digestion protocols, or protocols using only SDC or only C18 Empore™ disks. The advantages of the new protocol are demonstrated for two different types of samples: Merino wool intermediate filament proteins and Elaeis guineensis (oil palm) mesocarp proteins.