Beta Decay Studies of Nuclides in the Heavy Region

In the present work we studied the β-decay of various isotopes in the heavy region using the empirical formula of Fiset and Nix. It is found from the half-life that as the neutron number increases the possibility of β-decay increases. From the dependence of beta decay half-life on neutron number of parent and Q-value, we modified empirical formula of Fiset and Nix for beta decay half-life. We also developed an empirical formula for the Z-value of most stable isobar against β-decay. From the study of mass parabola for different isobars with mass number ranging from 200-223 it was found that the lowest point in the parabola, which is the Z-value of most stable isobar against β-decay, matches well with our formula predictions

Semi Empirical Formula For Neutrinoless Double Beta Decay

A Semi empirical formula for both phase space factor and Nuclear Matrix Element (NME) is developed for neutrinoless double beta decay, and the formula is used to compute the neutrinoless double beta decay half lives. Thecomputed half lives for neutrinoless double beta decay are compared with the corresponding experimental values and with those predicted by QRPA model. The semi empirical formula predictions are found to be in good agreement with experimental data. The semi empirical formula is used to predict neutrinoless double beta decay of various isotopes Ca, Ge, Se, Zr, Mo, Pd, Cd, Sn, Te, Xe, Nd and Sm that exhibiting single beta decay. As our semi empirical formula predictions agree with the experimental data we hope that the present work will be useful for the future experiments

Identifying polyglutamine protein species in situ that best predict neurodegeneration.

Polyglutamine (polyQ) stretches exceeding a threshold length confer a toxic function to proteins that contain them and cause at least nine neurological disorders. The basis for this toxicity threshold is unclear. Although polyQ expansions render proteins prone to aggregate into inclusion bodies, this may be a neuronal coping response to more toxic forms of polyQ. The exact structure of these more toxic forms is unknown. Here we show that the monoclonal antibody 3B5H10 recognizes a species of polyQ protein in situ that strongly predicts neuronal death. The epitope selectively appears among some of the many low-molecular-weight conformational states assumed by expanded polyQ and disappears in higher-molecular-weight aggregated forms, such as inclusion bodies. These results suggest that protein monomers and possibly small oligomers containing expanded polyQ stretches can adopt a conformation that is recognized by 3B5H10 and is toxic or closely related to a toxic species