Nanostructure and giant Hall effect in TMx(SiO2)(1-x) (TM=Co,Fe,Ni) granular system

Granular TMx(SiO2)(1-x) (TM=Co,Fe,Ni) thin films were thermally treated at different temperatures and their magnetotransport and structural properties were studied. Hall resistivity decreases with thermal annealing. Structure was analyzed based on small angle x-ray scattering results. A model of polydisperse system of hard spheres was used for obtaining structural parameters. Analysis reveals that a volume fraction of transition-metal atoms (less than 29%) are forming nanospheres. Changes in giant Hall effect upon annealing can depend on a particular combination of nanoparticle diameter, interparticle distance, and size distribution. (C) 2006 American Institute of Physics.99

Two new sealed sample cells for small angle x-ray scattering from macromolecules in solution and complex fluids using synchrotron radiation

Two different vacuum tight sample cells for in situ temperature dependent small angle scattering from liquids are presented in this article. In the first one, the sample fills a 1 mm thickness gap sealed on both sides by two thin parallel mica windows (volume 300 mul). In the second one, the liquid is injected into a 1 mm cylindrical capillary tube (volume 130 mul). The cells are lodged into temperature controlled chambers directly connected to the beamline vacuum path. Several important improvements with respect to similar instrumentation previously reported are: (1) versatile application of the mica cell, that can be used for all types of samples (gels, liquid crystals, and dispersions in organic solvents) and (2) the design of the chamber for the capillary cell allows registration of wider angle data and a convenient replacement of the capillary tube after each experiment. Signal to background ratio and data reproducibility were tested using protein solutions. We give a brief report of scattering experiments performed with different protein samples and two-dimensional data collection. (C) 2004 American Institute of Physics.75114541454

A New Euler's Formula for DNA Polyhedra

DNA polyhedra are cage-like architectures based on interlocked and interlinked DNA strands. We propose a formula which unites the basic features of these entangled structures. It is based on the transformation of the DNA polyhedral links into Seifert surfaces, which removes all knots. The numbers of components , of crossings , and of Seifert circles are related by a simple and elegant formula: . This formula connects the topological aspects of the DNA cage to the Euler characteristic of the underlying polyhedron. It implies that Seifert circles can be used as effective topological indices to describe polyhedral links. Our study demonstrates that, the new Euler's formula provides a theoretical framework for the stereo-chemistry of DNA polyhedra, which can characterize enzymatic transformations of DNA and be used to characterize and design novel cages with higher genus

The Pyrococcus exosome complex - Structural and functional characterization

The exosome is a conserved eukaryotic enzymatic complex that plays an essential role in many pathways of RNA processing and degradation. Here, we describe the structural characterization of the predicted archaeal exosome in solution using small angle x-ray scattering. The structure model calculated from the small angle x-ray scattering pattern provides an indication of the existence of a disk-shaped structure, corresponding to the "RNases PH ring" complex formed by the proteins aRrp41 and aRrp42. The RNases PH ring complex corresponds to the core of the exosome, binds RNA, and has phosphorolytic and polymerization activities. Three additional molecules of the RNA-binding protein aRrp4 are attached to the core as extended and flexible arms that may direct the substrates to the active sites of the exosome. In the presence of aRrp4, the activity of the core complex is enhanced, suggesting a regulatory role for this protein. The results shown here also indicate the participation of the exosome in RNA metabolism in Archaea, as was established in Eukarya.281106751675

Low resolution structure and stability studies of human GrpE#2, a mitochondrial nucleotide exchange factor

GrpE acts as a nucleotide exchange factor for the Hsp70 chaperone system. Only one GrpE isoform is present in Escherichia coli, but for reasons not yet well understood, two GrpE isoforms have been found in mammalian mitochondria. Therefore, studies aimed at evaluating the physico-chemical characteristics of these proteins are important for the comprehension of the function of the Hsp70 chaperone system in different organisms. Here we report biophysical studies on human mitochondrial GrpE isoform 2. Small angle X-ray scattering measurements of human GrpE isoform 2 showed that this protein has a quaternary structure which is similar to those of human GrpE isoform I and E coli GrpE: a dimer with a cruciform elongated shape. However, mitochondrial isoforms differed from each other regarding chemical and thermal denaturation profiles. This fact, combined with results of distinct expression patterns previously reported, point out that these proteins may have different response to external stimuli. Our results also indicate that human GrpE isoform 2 is more similar to the GrpE from E coli than to human GrpE isoform 1. These results are relevant because differences in the conformation of Hsp70 co-chaperones are considered to be one of the reasons for functional diversity of this system. (c) 2006 Elsevier Inc. All rights reserved.44941671778

Calorimetric and structural investigation of the interaction of lysozyme and bovine serum albumin with poly(ethylene oxide) and its copolymers

This work reports investigations aiming at verifying the occurrence of specific interactions between lysozyme or bovine serum albumin (BSA) and poly(ethylene oxide) and its copolymers with poly(propylene oxide). Thermal stability of these proteins, followed by means of high sensitivity DSC, was found to be mostly unaffected by the presence of these polymers. Chromatographic experiments (reverse-phase HPLC and size exclusion chromatrography) did not reveal any sign of specific interaction for these mixtures, either. Isothermal titration calorimetry revealed an increase in enthalpy for the mixtures, represented by a positive enthalpy of transfer for these proteins from buffer to polymer solutions. Moreover, SAXS analyses confirmed that at ambient temperatures these polymers do not affect lysozyme structure. In summary, no evidence is found to support earlier suggestions that some kind of complex could be formed between these proteins and poly(ethylene oxide) or its copolymers, but the present results suggest the occurrence of entropically driven hydrophobic effects. (C) 2004 Elsevier B.V. All rights reserved.3841671677

Folding and stability of the extracellular domain of the human amyloid precursor protein

The beta-amyloid peptide (Abeta), the major component of the senile plaques found in the brains of Alzheimer's disease patients, is derived from proteolytic processing of a transmembrane glycoprotein known as the amyloid precursor protein (APP). Human APP exists in various isoforms, of which the major ones contain 695, 751, and 770 amino acids. Proteolytic cleavage of APP by alpha- or beta-secretases releases the extracellular soluble fragments sAPPalpha or sAPPbeta, respectively. Despite the fact that sAPPalpha plays important roles in both physiological and pathological processes in the brain, very little is known about its structure and stability. We have recently presented a structural model of sAPPalpha(695) obtained from small-angle x-ray scattering measurements (Gralle, M., Botelho, M. M., Oliveira, C. L. P., Torriani, I., and Ferreira, S. T. ( 2002) Biophys. J. 83, 3513 - 3524). We now report studies on the folding and stabilities of sAPPalpha(695) and sAPPalpha(770). The combined use of intrinsic fluorescence, 4-4'-Dianilino-1,1' binaphthyl-5,5'-disulfonic acid ( bis-ANS) fluorescence, circular dichroism, differential ultraviolet absorption, and small-angle x-ray scattering measurements of the equilibrium unfolding of sAPPalpha(695) and sAPPalpha(770) by GdnHCl and urea revealed multistep folding pathways for both sAPPalpha isoforms. Such stepwise folding processes may be related to the identification of distinct structural domains in the three-dimensional model of sAPPalpha. Furthermore, the relatively low stability of the native state of sAPPalpha suggests that conformational plasticity may play a role in allowing APP to interact with a number of distinct physiological ligands.27836342593426