Testing the mechanism for the LSP stability at the LHC

The lightest supersymmetric particle (LSP) is a natural candidate for the cold dark matter of the universe. In this Letter we discuss how to test the mechanism responsible for the LSP stability at the LHC. We note that if R-parity is conserved dynamically one should expect a Higgs boson which decays mainly into two right-handed neutrinos (a “leptonic” Higgs) or into two sfermions. The first case could exhibit spectacular lepton number violating signals with four secondary vertices due to the long-lived nature of right-handed neutrinos. These signals, together with the standard channels for the discovery of SUSY, could help to establish the underlying theory at the TeV scale.     

Neuropeptide delivery to the brain: a von Willebrand factor signal peptide to direct neuropeptide secretion

Background  

Multiple neuropeptides, sometimes with opposing functions, can be produced from one precursor gene. To study the roles of the different neuropeptides encoded by one large precursor we developed a method to overexpress minigenes and establish local secretion.     

A numerical validation approach of a finite element muscle model using optical data

Aim of this work is to obtain a convenient data set for the validation of a recently developed three-dimensional constitutive muscle model. Therefore, an optical measurement technique is used to reconstruct a geometrical model of a rabbit soleus muscle. Thus, the muscle geometry and also the generated force characteristics are measured. The proposed numerical model is able to reproduce the experimental results in an adequate manner. (© 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim)     

Decoding the Fucose Migration Product during Mass-Spectrometric analysis of Blood Group Epitopes

Fucose is a signaling carbohydrate that is attached at the end of glycan processing. It is involved in a range of processes, such as the selectin-dependent leukocyte adhesion or pathogen-receptor interactions. Mass-spectrometric techniques, which are commonly used to determine the structure of glycans, frequently show fucose-containing chimeric fragments that obfuscate the analysis. The rearrangement leading to these fragments—often referred to as fucose migration—has been known for more than 25 years, but the chemical identity of the rearrangement product remains unclear. In this work, we combine ion-mobility spectrometry, radical-directed dissociation mass spectrometry, cryogenic IR spectroscopy of ions, and density-functional theory calculations to deduce the product of the rearrangement in the model trisaccharides Lewis x and blood group H2. The structural search yields the fucose moiety attached to the galactose with an α(1→6) glycosidic bond as the most likely product.