CoFeB/MgO/CoFeB structures with orthogonal easy axes: perpendicular anisotropy and damping.

We report on the Gilbert damping parameter α, the effective magnetization [Formula: see text], and the asymmetry of the g-factor in bottom-CoFeB(0.93 nm)/MgO(0.90-1.25 nm)/CoFeB(1.31 nm)-top as-deposited systems. Magnetization of CoFeB layers exhibits a specific noncollinear configuration with orthogonal easy axes and with [Formula: see text] values of [Formula: see text] kG and [Formula: see text] kG for the bottom and top layers, respectively. We show that [Formula: see text] depends on the asymmetry [Formula: see text] of the g-factor measured in the perpendicular and the in-plane directions revealing a highly nonlinear relationship. In contrast, the Gilbert damping is practically the same for both layers. Annealing of the films results in collinear easy axes perpendicular to the plane for both layers. However, the linewidth is strongly increased due to enhanced inhomogeneous broadening.

Determination of the spin torque non-adiabaticity in perpendicularly magnetized nanowires.

Novel nanofabrication methods and the discovery of an efficient manipulation of local magnetization based on spin polarized currents has generated a tremendous interest in the field of spintronics. The search for materials allowing for fast domain wall dynamics requires fundamental research into the effects involved (Oersted fields, adiabatic and non-adiabatic spin torque, Joule heating) and possibilities for a quantitative comparison. Theoretical descriptions reveal a material and geometry dependence of the non-adiabaticity factor ß, which governs the domain wall velocity. Here, we present two independent approaches for determining ß: (i) measuring the dependence of the dwell times for which a domain wall stays in a metastable pinning state on the injected current and (ii) the current-field equivalence approach. The comparison of the deduced ß values highlights the problems of using one-dimensional models to describe two-dimensional dynamics and allows us to ascertain the reliability, robustness and limits of the approaches used.

The search for DNA homology does not limit stable homologous pairing promoted by RecA protein.

BACKGROUND: The basic molecular mechanisms that govern the search for DNA homology and subsequent homologous pairing during genetic recombination are not understood. RecA is the central homologous recombination protein of Escherichia coli; because several RecA homologues have been identified in eukaryotic cells, it is likely that the mechanisms employed by RecA are conserved throughout evolution. Analysis of the kinetics of the homologous search and pairing reactions catalyzed by RecA should therefore provide insights of general relevance into the mechanisms by which macromolecules locate, and interact with, specific DNA targets. RESULTS: RecA forms three-stranded synaptic complexes with a single-stranded oligonucleotide and a homologous region in duplex DNA. The kinetics of this initial pairing reaction were characterized using duplex DNA molecules of various concentrations and complexities containing a single target site, as well as various concentrations of homologous single-stranded oligonucleotides. The formation of the synaptic complex follows apparent second-order reaction kinetics with a rate proportional to the concentrations of both the homologous single-stranded oligonucleotide and the target sites within the duplex DNA. The reaction rate is independent of the complexity of duplex DNA in the reaction. We propose a kinetic scheme in which the RecA-single-stranded DNA filament interacts with duplex DNA and locates its target in a relatively fast reaction. We also suggest that complex conformational changes occur during the subsequent rate-limiting step. CONCLUSIONS: We conclude that, during the formation of synaptic complexes by RecA, the search for homology is not rate-limiting, and that the iteration frequency of the search is around 10(2)-10(3) s-1. This value agrees well with what has been calculated as the minimum number for such a frequency in genome-wide searches, and limits the possible structures involved in the search for homology to those involving very soft (low energy) interactions. Furthermore, from the order of the reaction at the DNA concentrations found in eukaryotic nuclei, and the rate constant of the overall reaction, we predict that the search for homology is also not the rate-limiting step in the genome-wide searches implicated in meiosis and in gene targeting.

Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases.

A partial duplex DNA substrate containing the Lac repressor binding site, within the duplex region, was constructed to examine the effect of bound Lac repressor on the unwinding reaction catalyzed by several DNA helicases. The substrate contained 90 base pairs of double-stranded DNA and, in the absence of Lac repressor, was effectively unwound by each of the seven helicases tested. The unwinding reactions catalyzed by Escherichia coli Rep protein, bacteriophage T4 Dda protein and E. coli DNA helicase I were not inhibited by the presence of bound Lac repressor. Both SV40 T antigen and E. coli helicase II were partially inhibited by bound repressor at the highest repressor concentrations tested. The helicase reactions catalyzed by E. coli DnaB protein and helicase IV were substantially inhibited by the presence of bound protein. When the length of the duplex region was increased to 323 base pairs the inhibition spectrum caused by bound Lac repressor on the unwinding reactions catalyzed by DnaB protein, helicase I and helicase II was essentially the same as that observed using the shorter partial duplex molecule. Inhibition of the unwinding reaction was due to the presence of bound Lac repressor as evidenced by the substantially weaker inhibition of helicase IV by Lac repressor in the presence of IPTG. In addition, we have shown that Rep protein displaces the bound repressor protein during the course of an unwinding reaction.

Escherichia coli Rep protein and helicase IV. Distributive single-stranded DNA-dependent ATPases that catalyze a limited unwinding reaction in vitro.

Rep protein and helicase IV, two DNA-dependent adenosine 5'-triphosphatases with helicase activity, have been purified from Escherichia coli and characterized. Both enzymes exhibit a distributive interaction with single-stranded DNA as DNA-dependent ATPases in a reaction that is relatively resistant to increasing NaCl concentration and sensitive to the addition of E. coli single-stranded DNA binding protein (SSB). The helicase reaction catalyzed by each protein has been characterized using a direct unwinding assay and partial duplex DNA substrates. Both Rep protein and helicase IV catalyzed the unwinding of a duplex region 71 bp in length. However, unwinding of a 119-bp or 343-bp duplex region was substantially reduced compared to unwinding of the 71-bp substrate. At each concentration of protein examined, the number of base pairs unwound was greatest using the 71-bp substrate, intermediate with the 119-bp substrate and lowest using the 343-bp substrate. The addition of E. coli SSB did not increase the fraction of the 343-nucleotide fragment unwound by Rep protein. However, the addition of SSB did stimulate the unwinding reaction catalyzed by helicase IV approximately twofold. In addition, ionic strength conditions which stabilize duplex DNA (i.e. addition of MgCl2 or NaCl), markedly inhibited the helicase reaction catalyzed by either Rep protein or helicase IV while having little effect on the ATPase reaction. Thus, these two enzymes appear to share a common biochemical mechanism for unwinding duplex DNA which can be described as limited unwinding of duplex DNA. Taken together these data suggest that, in vitro, and in the absence of additional proteins, neither Rep protein nor helicase IV catalyzes a processive unwinding reaction.

Pyridazino[1,2-a] 1,2,5-triazepines.

By the condensation of 1,2-di(chloracetyl)piperidazine with primary amines 3-substituted derivatives of 1,5-diketoperhydropyridazino[1,2-a] 1,2,5-triazepine (1--8, Fig. 1) were obtained. Some of them show sedative action at the 25--100 mg/k dosis level and are of low ip toxicity.