Estudo de métodos de inoculação para a avaliação de cultivares de soja a Fusarium tucumaniae

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

Structural characterization and Curie temperature determination of a sodium strontium niobate ferroelectric nanostructured powder

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

Loss in tocopherols and oxidative stability during the frying of frozen cassava chips

The present study was aimed at verifying tocopherols losses and oxidative stability changes in vegetable oils used in discontinuous frying. The frying of frozen cassava chips was carried out in a household electric frying pan, where the oil was heated to a temperature of 180 degrees C for 25 hours, with fresh oil replacement. The results obtained from the analytical determinations were submitted to variance analysis, in a factorial scheme, using a completely randomized design, making it possible to determine the influence of the type of oil and frying times on changes in the oil. The data show that the smallest changes occur in palm oil, which is more saturated. For sunflower and cottonseed oils, which are more unsaturated, there was a clear decrease in both tocopherol concentration and oxidative stability.

The Origin of Nonmonotonic Complex Behavior and the Effects of Nonnative Interactions on the Diffusive Properties of Protein Folding

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

SAXS study of crotapotin at low pH

The structure of crotapotin, a protein extracted from the venom of the Crotalus durissus terrificus, in solution at pH = 1.5, was studied by SAXS. The experimental results yield structural parameter values of the molecular radius of gyration R(g) = 13.6 angstrom, volume v = 16.2 x 10(3) angstrom3 and maximal dimension D(max) = 46 angstrom. The distance distribution function deduced from the scattering measurements is consistent with an overall molecular shape of an oblate ellipsoid of revolution with assymetry parameter nu = 0.45.

Computational studies of the reversible domain swapping of p13suc1

A minimalist representation of protein structures using a Go- like potential for interactions is implemented to investigate the mechanisms of the domain swapping of p13suc1, a protein that exists in two native conformations: a monomer and a domain- swapped dimer formed by the exchange of a beta- strand. Inspired by experimental studies which showed a similarity of the transition states for folding of the monomer and the dimer, in this study we justify this similarity in molecular descriptions. When intermediates are populated in the simulations, formation of a domain- swapped dimer initiates from the ensemble of unfolded monomers, given by the fact that the dimer formation occurs at the folding/ unfolding temperature of the monomer ( T-f). It is also shown that transitions, leading to a dimer, involve the presence of two intermediates, one of them has a dimeric form and the other is monomeric; the latter is much more populated than the former. However, at temperatures lower than T-f, the population of intermediates decreases. It is argued that the two folded forms may coexist in absence of intermediates at a temperature much lower than T-f. Computational simulations enable us to find a mechanism, `` lock- and- dock'', for domain swapping of p13suc1. To explore the route toward dimer formation, the folding of unstructured monomers must be retarded by first locking one of the free ends of each chain. Then, the other free termini could follow and dock at particular regions, where most intrachain contacts are formed, and thus de. ne the transition states of the dimer. The simulations also showed that a decrease in the maximum distance between monomers increased their stability, which is explained based on confinement arguments. Although the simulations are based on models extracted from the native structure of the monomer and the dimer of p13suc1, the mechanism of the domain- swapping process could be general, not only for p13suc1.