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The detection and positive identification of the short-lived, low cross section isotopes used in the chemical studies of the heaviest elements are usually accomplished by measuring their alpha-decay, thus the nuclear properties of the heaviest elements must be examined simultaneously with their chemical properties. The isotopes 224 Pa and 266,267 Bh have been studied extensively as an integral part of the investigation of the heaviest members of the groups five and seven of the periodic table. The half-life of 224 Pa was determined to be 855 plus/minus19 ms by measuring its alpha-decay using our rotating wheel, solid state detector system at the Lawrence Berkeley National Laboratory 88-Inch Cyclotron. Protactinium was produced by bombardment of a bismuth target. New neutron rich isotopes, 267 Bh and 266 Bh, were produced in bombardments of a 249 Bk target and their decay was observed using the rotating wheel system. The 266 Bh that was produced decays with a half-life of approximately 1 s by emission of alpha particles with an average energy of 9.25 plus/minus 0.03 MeV. 267 Bh was observed to decay with a 17 s half-life by emission of alpha-particles with an average energy of 8.83 plus/minus 0.03 MeV. The chemical behavior …

Multidimensional heteronuclear NMR spectroscopy was used to investigate the N-terminal domain of the transcriptional enhancer NTRC (NiTrogen Regulatory protein C). This domain belongs to the family of receiver domains of two-component regulatory systems involved in signal transduction. Phosphorylation of NTRC at D54 leads to an activated form of the molecule which stimulates transcription of genes involved in nitrogen regulation. Three and four dimensional NMR techniques were used to determine an intermediate resolution structure of the unphosphorylated, inactive form of the N-terminal domain of NTRC. The structure is comprised of five {alpha}-helices and a five-stranded {beta}-sheet in a ({beta}/{alpha}){sub 5} topology. Analysis of the backbone dynamics of NTRC indicate that helix 4 and strand 5 are significantly more flexible than the rest of the secondary structure of the protein and that the loops making up the active site are flexible. The short lifetime of phospho-NTRC hampers the study of this form. However, conditions for determining the resonance assignments and, possibly, the three dimensional structure of phosphorylated NTRC have been obtained. Tentative assignments of the phosphorylated form indicate that the majority of the changes that NTRC experiences upon phosphorylation occur in helix 3, strand 4, helix 4, strand 5, and the loop …