Effect of bound nucleon internal structure change on nuclear structure functions

Effect of bound nucleon internal structure change on nuclear structure functions is investigated based on local quark-hadron duality. The bound nucleon structure functions calculated for charged-lepton and (anti)neutrino scattering are all enhanced in symmetric nuclear matter at large Bjorken-x (x greater than or similar to 0.85) relative to those in a free nucleon. This implies that a part of the enhancement observed in the nuclear structure function F-2 (in the resonance region) at large Bjorken-x (the EMC effect) is due to the effect of the bound nucleon internal structure change. However, the x dependence for the charged-lepton and (anti)neutrino scattering is different. The former (latter) is enhanced (quenched) in the region 0.8 less than or similar to x less than or similar to 0.9 (0.7 less than or similar to x less than or similar to 0.85) due to the difference of the contribution from axial vector forrn factor. Because of these differences charge symmetry breaking in parton distributions will be enhanced in nuclei. (c) 2005 Elsevier B.V. All rights reserved.

Targeted Nucleotide Exchange in Bovine Myostatin Gene

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Qualidade estrutural de um latossolo vermelho submetido à compactação

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Invasive Africanized honeybees change the structure of native pollination networks in Brazil

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Genetic diversity and population structure of pumas (Puma concolor) in southeastern Brazil: implications for conservation in a human-dominated landscape

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

THE EFFECT of CARBONIZATION on WOOD STRUCTURE of DALBERGIA VIOLACEA, STRYPHNODENDRON POLYPHYLLUM, TAPIRIRA GUIANENSIS, VOCHYSIA TUCANORUM, and POUTERIA TORTA FROM THE BRAZILIAN CERRADO

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Structural, electronic structure and magnetic studies of GdFe1-xNixO3 (x <= 0.5)

The structural, electronic structure and magnetic properties of Ni doped GdFeO3 perovskite materials have been studied. A decreasing trend in volume with the increasing Ni concentration without any structural change is confirmed from X-ray diffraction studies. The electronic structural studies show that the competing ions within the ensemble have +3 oxidation states, which includes the Gd, Fe and Ni ions, and also confirms the octahedral symmetry of the Fe/Ni ions. The magnetic properties clearly depict that the Ni doping can tailor the phase transitions arising due to temperature/field dependence having a heavy impact on spin dynamics. (C) 2012 Elsevier B.V. All rights reserved.

A tellurium-based cathepsin B inhibitor: Molecular structure, modelling, molecular docking and biological evaluation

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

The structure and optical dispersion of the refractive index of tellurite glass

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Change of the vortex lattice symmetry in the vicinity of the macro-to-mesoscopic threshold

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Population dynamics, structure and behavior of Anopheles darlingi in a rural settlement in the Amazon rainforest of Acre, Brazil

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Population dynamics, sex ratio and size at sex change in a protandric simultaneous hermaphrodite, the spiny shrimp Exhippolysmata oplophoroides

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis

The 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds and is absent in mammals, which makes it a potential target for drugs development against microbial diseases. Here, we report the phosphate binding effects at the structure of the 5-enolpyruvyl shikimate-3-phosphate synthase from Mycobacterium tuberculosis. This enzyme is formed by two similar domains that close on each other induced by ligand binding, showing the occurrence of a large conformation change. We have monitored the phosphate binding effects using analytical ultracentrifugation, small angle X-ray scattering and, circular dichroism techniques. The low resolution results showed that the enzyme in the presence of phosphate clearly presented a more compact structure. Thermal-induced unfolding experiments followed by circular dichroism suggested that phosphate rigidified the enzyme. Summarizing, these data suggested that the phosphate itself is able to induce conformational change resulting in the closure movement in the M. tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase. (c) 2006 Elsevier B.V. All rights reserved.

A seasonally dependent change in the distribution and physiological condition of Caiman crocodilus yacare in the Paraguay River Basin

The distribution and physiological condition of 116 Caiman crocodilus yacare was assessed over one year in the Southern Pantanal. Body mass and intermediary plasma metabolites were measured at three different time periods, representing large differences in the abundance of surface water. During the wet season the study site was completely submerged under water and C. c. yacare were distributed evenly throughout. High levels of [glucose] and [triglyceride] in the plasma indicated regular feeding. As the dry season progressed C. c. yacare became increasingly crowded around the remaining ponds. They showed a reduction in plasma [glucose] and [triglyceride], and an increase in plasma [beta-hydroxy-butyrate], signifying that they were feeding less and utilising fat reserves. At this sampling period, similar to 40% of the male C. c. yacare that were > 10 years old inhabited dry grassland and did not have access to water. These animals were significantly lighter than males of a similar length that had immediate water access, and plasma [uric acid] indicated that they had not fed for a long time and were metabolising tissue proteins. Essentially, the adult male C. c. yacare that inhabited dry grassland were in a state of energy deficiency. This was so severe in some animals that recovery seemed unlikely. The study suggests that fluctuations in the abundance of surface ground water may influence the size and structure of the C. c. yacare population in the Pantanal.

Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1)

The 1.7 angstrom resolution crystal structure of recombinant family G/11 beta-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved P-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328 K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298-328 K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328 K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.