Particle shape in thixotropic aluminium and thorium molybdates gels

Summary Electron microscope examination of thixotropic aluminium and thorium molybdate gels shows that one hour after formation they are constituted by short fibrils of small axial ratio. The fibrils of the aluminium molybdate gels, with ageing at room temperature or with boiling, increase in diameter and length; the fibrous shape of the particles is maintained after two and a half years of ageing; all fibrils are crystalline by electron diffraction. The fibrils of the thorium molybdate gels, except in the gels containing hydrochloric acid, change with ageing at room temperature or with boiling, into plates of hexagonal, elliptical or rectangular profile; the fibrils and plates are crystalline and have the same electron diffraction pattern as the fibrils.This work was aided, in part, by grants from Conselho Nacional de Pesquisas and the Rockefeller Foundation.     

The cardinalities of the Green classes of the free objects in varieties of bands

We compute the cardinalities of the Green classes of the free objects in the varieties of bands. We also compare the cardinalities obtained and analyse the “collapsing” of the finitely generated free objects. We deduce corresponding results for varieties of band monoids.     

Surface Science: Foundations of Catalysis and Nanoscience

Journal of Nanoparticle Research -     

On some Nikolski - and Oswald-type inequalities

Inequalities of Nikolski (Trudy Mat. Inst. Steklova 38 (1951), 2.3, p. 255) in L_2π^p, p 1, and of Oswald (Izv. Vyssh. Uchebn. Zaved. Mat. 7 (1976), (3.4), p. 71; Theorem 1, p. 69), 0 < p < 1, are extended to the case of Orlicz spaces L_2π.     

The equality of fractal dimension and uncertainty dimension for certain dynamical systems

[MGOY] introduced the uncertainty dimension as a quantative measure for final state sensitivity in a system. In [MGOY] and [P] it was conjectured that the box-counting dimension equals the uncertainty dimension for basin boundaries in typical dynamical systems. In this paper our main result is that the box-counting dimension, the uncertainty dimension and the Hausdorff dimension are all equal for the basin boundaries of one and two dimensional systems, which are uniformly hyperbolic on their basin boundary. When the box-counting dimension of the basin boundary is large, that is, near the dimension of the phase space, this result implies that even a large decrease in the uncertainty of the position of the initial condition yields only a relatively small decrease in the uncertainty of which basin that initial point is in.Research in part supported by AFOSR and by the Department of Energy (Scientific Computing Staff Office of Energy Research)     

New fused pyrroles with rA1/A2A antagonistic activity as potential therapeutics for neurodegenerative disorders

Molecular Diversity - In a pilot study, eleven pyrrolopyridine and pyrrolopyrimidine derivatives (specifically, 7-azaindole and 7-deazapurine derivatives) were synthesised by Suzuki cross-coupling...     

Yttrium aluminate crystals for slabs

The methods of growing YAG:Nd crystals with a flat interface and YAP:Nd crystals with a sharp conical interface are described. The form of the interface was controlled by the He and H₂O content in the reducing atmosphere composed mainly of Ar and H₂ as well as by axial temperature gradient above the melt level. The crystals of 120–180 mm in length were machined to the high-quality slabs.     

EPR spectroscopy of protein microcrystals oriented in a liquid crystalline polymer medium

Correlation of the g-tensor of a paramagnetic active center of a protein with its structure provides a unique experimental information on the electronic structure of the metal site. To address this problem, we made solid films containing metalloprotein (Desulfovibrio gigas cytochrome c(3)) microcrystals. The microcrystals in a liquid crystalline polymer medium (water/hydroxypropylcellulose) were partially aligned by a shear flow. A strong orientation effect of the metalloprotein was observed by EPR spectroscopy and polarizing optical microscopy. The EPR spectra of partially oriented samples were simulated, allowing for molecular orientation distribution function determination. The observed effect results in enhanced sensitivity and resolution of the EPR spectra and provides a new approach towards the correlation of spectroscopic data, obtained by EPR or some other technique, with the three-dimensional structure of a protein or a model compound.