Investigation of cold fusion in heavy water

An investigation of cold fusion of deuterium was performed by electrolyzing heavy water in a cell containing a palladium cathode while monitoring levels of tritium and neutron-capture gamma rays. No activity was detected that would indicate a sustained fusion reaction had taken place. Activities that were observed can be attributed to electrolytic enrichment and a normal cosmic-ray induced background.     

Darstellung und Kristallstruktur von Bis(heptaquocalcium)-dekachlorodithallat(III) [Ca(OH2)7]2TI2Cl10

Preparation and Crystal Structure of Bis(heptaquocalcium)-decachlorodithallat(III) [Ca(OH₂)₇]₂Tl₂Cl₁₀ Colourless, hygroscopic crystals of the compound CaTlCl₅ · 7H₂O were obtained by crystallization from aqueous solutions of CaCl₂ and TlCl₃. The crystal structure consists of [Ca(OH₂)₇]²⁺ cations and [Tl₂Cl₁₀]^4?anions.     

Acrolein and Copper as Competitive Effectors of α-Synuclein

Mounting evidence supports the role of amyloidogenesis, oxidative stress, and metal dyshomeostasis in the development of neurodegenerative disorders. Parkinson's Disease is characterized by α-synuclein (αSyn) accumulation and aggregation in brain regions, also promoted by Cu²⁺. αSyn is modified by reactive carbonyl species, including acrolein (ACR). Notwithstanding these findings, the interplay between ACR, copper, and αSyn has never been investigated. Therefore, we explored more thoroughly the effects of ACR on αSyn using an approach based on LC-MS/MS analysis. We also evaluated the influence of Cu²⁺ on the protein carbonylation and how the ACR modification impacts the Cu²⁺ binding and the production of Reactive Oxygen Species (ROS). Finally, we investigated the effects of ACR and Cu²⁺ ions on the αSyn aggregation by dynamic light scattering and fluorescence assays. Cu²⁺ regioselectively inhibits the modification of His50 by ACR, the carbonylation lowers the affinity of His50 for Cu²⁺ and ACR inhibits αSyn aggregation both in the presence and in the absence of Cu²⁺.     

The raspberry model for protein-like particles: Ellipsoids and confinement in cylindrical pores

The study of protein mass transport via atomistic simulation requires time and length scales beyond the computational capabilities of modern computer systems. The raspberry model for colloidal particles in combination with the mesoscopic hydrodynamic method of lattice Boltzmann facilitates coarse-grained simulations that are on the order of microseconds and hundreds of nanometers for the study of diffusive transport of protein-like colloid particles. The raspberry model reproduces linearity in resistance to motion versus particle size and correct enhanced drag within cylindrical pores at off-center coordinates for spherical particles. Owing to the high aspect ratio of many proteins, ellipsoidal raspberry colloid particles were constructed and reproduced the geometric resistance factors of Perrin and of Happel and Brenner in the laboratory-frame and in the moving body-frame. Accurate body-frame rotations during diffusive motion have been captured for the first time using projections of displacements. The spatial discretization of the fluid leads to a renormalization of the hydrodynamic radius, however, the data describes a self-consistent hydrodynamic frame within this renormalized system.