31P-nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

Abstract31P-nuclear magnetic resonance spectra were obtained from intact plasmodial cells of Physarum polycephalum, where cytoplasmic streaming is generated by actin-myosin-ATP interaction. Several peaks were resolved and identified. They included ATP, ADP, orthophosphate and polyphosphates. Peaks for phosphocreatine, phosphoarginine or AMP were not detected. The intracellular pH and concentrations of ATP and free Mg2+ were estimated to be pH 6.9, 0.2–0.5 mM, and about 1 mM, respectively

Difference between interaction cross sections and reaction cross sections

We revisit the commonly accepted notion that the difference between interaction and reaction cross sections is negligible at relativistic energies, and show that, especially in small mass number region, it is large enough to help probe nuclear structure. For analyses of the difference, we construct "pseudo data" for the reaction cross sections using a phenomenological black-sphere model of nuclei since empirical data are very limited at high energies. The comparison with the empirical interaction cross sections suggests a significant difference between the reaction and interaction cross sections for stable projectiles on a carbon target, which is of the order of 0-100 mb.Comment: 5 pages, 5 figure

Application of Poly(amidoamine) Dendrimers for Use in Bionanomotor Systems

The study and utilization of bionanomotors represents a rapid and progressing field of nanobiotechnology. Here, we demonstrate that poly(amidoamine) (PAMAM) dendrimers are capable of supporting heavy meromyosin dependent actin motility of similar quality to that observed using nitrocellulose, and that microcontact printing of PAMAM dendrimers can be exploited to produce tracks of active myosin motors leading to the restricted motion of actin filaments across a patterned surface. These data suggest that the use of dendrimer surfaces will increase the applicability of using protein biomolecular motors for nanotechnological applications

The fastest-actin-based motor protein from the green algae, Chara, and its distinct mode of interaction with actin

AbstractThe endoplasmic streaming in Characean cells is an actin-dependent movement. The motor protein responsible for the streaming was partially purified and characterized. It was soluble at low ionic strength, an ATPase of a molecular mass of 225 kDa and activated more than 100 times by muscle F-actin. Surprisingly, in an in vitro motility assay, the motor protein moved muscle F-actin at 60 μm/s, which is similar to the velocity of streaming in a living cell and 10 times faster than muscle myosin. Proteolytic cleavage of actin impaired movement crucially on muscle myosin, but did not affect movement at all on the Chara motor protein, suggesting that the Chara motor protein would interact with actin via a set of sites different from those of muscle myosin

Water budget and treating performance in the treatment of high salinity landfill leachate with two stage of hybrid constructed wetlands

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