The periodic Anderson model from the atomic limit and FeSi

The exact Green's functions of the periodic Anderson model for $U\to \infty$ are formally expressed within the cumulant expansion in terms of an effective cumulant. Here we resort to a calculation in which this quantity is approximated by the value it takes for the exactly soluble atomic limit of the same model. In the Kondo region a spectral density is obtained that shows near the Fermi surface a structure with the properties of the Kondo peak. Approximate expressions are obtained for the static conductivity $$ and magnetic susceptibility $\chi (T)$ of the PAM, and they are employed to fit the experimental values of FeSi, a compound that behaves like a Kondo insulator with both quantities vanishing rapidly for $T\to 0$. Assuming that the system is in the intermediate valence region, it was possible to find good agreement between theory and experiment for these two properties by employing the same set of parameters. It is shown that in the present model the hybridization is responsible for the relaxation mechanism of the conduction electrons.Comment: 26 pages and 8 figure

Evaluation of superovulatory response in Santa Inês ewes by ultrasonography and laparoscopy.

The development and use of non-invasive techniques would reduce risks of surgery sequels on the same animal and use of the donor could be optimized. The aim of this study was to evaluate the accuracy of ultrasonography performed prior to embryo collection to estimate superovulation response in sheep. Fifteen pluriparous Santa Inês sheep, 2 to 5 year old, with an average body weight of 46.79 ± 6.00 kg and body condition score of 2.96 ± 0.32 (1 to 5 scale) were allocated into 3 groups (GI, GII, GIII) in a cross-over design. In GI, intravaginal sponges (60 mg of medroxyprogesterone acetate; Progespon®, Schering Plough Animal Health, São Paulo, Brazil) were inserted (Day 0) and maintained for 14 days, and the superovulatory (SOV) protocol started on Day 12. In GII and GIII, intravaginal sponges were inserted (Day 0) and maintained for 6 days. On Day 5, the animals were treated with 300 IU of eCG (Novormon 5000®, Schering Plough Animal Health) and 5 mg of dinoprost (Lutalyse® Pfizer Animal Health, São Paulo, Brazil) i.m. Animals in GIII received 0.025 mg of gonadorelin acetate (Gestran-Plus®, Tecnopec, São Paulo, Brazil) i.m. 12 h after sponge withdrawal. In GII and GIII, the SOV protocol started 48 h after sponge removal and a new sponge was inserted immediately after its removal. The SOV protocol in all groups consisted of 200 mg of pFSH (Folltropin-V®, Tecnopec) administered in 6 decreasing doses given every 12 h (50/50, 30/30, and 20/20 mg). At the time of the fifth dose of pFSH, 5 mg of dinoprost was administered i.m. and the sponges were removed. Animals were bred by a sexually mature ram twice a day until the end of estrus. Prior to embryo collection, an ultrasonographic evaluation (5 MHz, Aloka SSD-500, Tokyo, Japan) was performed to determine the number of CL present on both ovaries. The number of CL was further evaluated by laparoscopy, when it was possible to detect poor responders or even non-ovulating animals. Statistical analysis was performed using all tests at the 95% confidence interval by SAEG program. Results are presented as mean ± SE. The number of CL was not different among all groups. The total number (GI, GII, and GIII) of CL determined by ultrasonography (9.09 ± 5.01) was not different (P > 0.05) from that observed by laparoscopy (8.87 ± 5.25). A significant correlation (r = 0.56, P < 0.0005) between evaluation performed by ultrasonography and laparoscopy was observed. These results suggest that ultrasonography can be used to determine the response to the superovulatory protocol. As embryo collection in sheep is performed mainly by surgical techniques, the implementation of non-invasive techniques such as ultrasonography could avoid unnecessary surgeries on animals that did not respond to the SOV protocol, therefore preventing early culling of embryo donors. Top Print this pagePrint Email this page View Issue Contents Abstract Export Citation Tools Print Bookmark Email this page Early Alert Subscribe to our Early Alerts for the latest journal issue contents.Edição dos Proceedings of the Annual Conference of the International Embryo Transfer Society, Córdoba, Argentina, 9?12 January 2010

Thermodynamic properties of the periodic Anderson model:X-boson treatment

We study the specific dependence of the periodic Anderson Model (PAM) in the limit of $U=\infty$ employing the X-boson treatment in two fifferent regimes of the PAM: the heavy fermion Kondo (HF-K) and the heavy fermion local magnetic regime (HF-LMM). We obtain a multiple peak structure for the specific heat in agreement with experimental results as well as the increase of the electronic effective mass at low temperatures associated with the HF-K regime. The entropy per site at low T tends to zero in the HF-K regime, corresponding to a singlet ground state, and it tends to $k_{B}ln(2)$ in the HF-LMM, corresponding to a doublet ground state at each site. The linear coefficient $\gamma(T)=C_{v}/T$ of the specific heat qualitatively agrees with the experimental results obtained for differents materials in the two regimes considered here.Comment: 9 pages, 14 figure

Low-Resolution Molecular Models Reveal the Oligomeric State of the PPAR and the Conformational Organization of Its Domains in Solution

The peroxisome proliferator-activated receptors (PPARs) regulate genes involved in lipid and carbohydrate metabolism, and are targets of drugs approved for human use. Whereas the crystallographic structure of the complex of full length PPARγ and RXRα is known, structural alterations induced by heterodimer formation and DNA contacts are not well understood. Herein, we report a small-angle X-ray scattering analysis of the oligomeric state of hPPARγ alone and in the presence of retinoid X receptor (RXR). The results reveal that, in contrast with other studied nuclear receptors, which predominantly form dimers in solution, hPPARγ remains in the monomeric form by itself but forms heterodimers with hRXRα. The low-resolution models of hPPARγ/RXRα complexes predict significant changes in opening angle between heterodimerization partners (LBD) and extended and asymmetric shape of the dimer (LBD-DBD) as compared with X-ray structure of the full-length receptor bound to DNA. These differences between our SAXS models and the high-resolution crystallographic structure might suggest that there are different conformations of functional heterodimer complex in solution. Accordingly, hydrogen/deuterium exchange experiments reveal that the heterodimer binding to DNA promotes more compact and less solvent-accessible conformation of the receptor complex