[Characterization and structural approach to crystalline La2O3-MgO-B2O3]. / Caractérisation et approche structurale de verres du systeme La2O3-MgO-B2O3.

In this paper, a vitreous domain of the ternary system: xLa2O3-yMgO-zB2O3 characterised by X-ray diffraction is shown. Structural approach using vibrational spectroscopy and optical probe is realized for some of these glasses and compared to crystalline LaMgB5O10.

A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure.

The solution structure of a new B-chain mutant of bovine insulin, in which the cysteines B7 and B19 are replaced by two serines, has been determined by circular dichroism, 2D-NMR and molecular modeling. This structure is compared with that of the oxidized B-chain of bovine insulin [Hawkins et al. (1995) Int. J. Peptide Protein Res.46, 424-433]. Circular dichroism spectroscopy showed in particular that a higher percentage of helical secondary structure for the B-chain mutant is estimated in trifluoroethanol solution in comparison with the oxidized B-chain. 2D-NMR experiments confirmed, among multiple conformations, that the B-chain mutant presents defined secondary structures such as a alpha-helix between residues B9 and B19, and a beta-turn between amino acids B20 and B23 in aqueous trifluoroethanol. The 3D structures, which are consistent with NMR data and were obtained using a simulated annealing protocol, showed that the tertiary structure of the B-chain mutant is better resolved and is more in agreement with the insulin crystal structure than the oxidized B-chain structure described by Hawkins et al. An explanation could be the presence of two sulfonate groups in the oxidized insulin B-chain. Either by their charges and/or their size, such chemical groups could play a destructuring effect and thus could favor peptide flexibility and conformational averaging. Thus, this study provides new insights on the folding of isolated B-chains.

Structural modification on silica glass surface induced by thermal poling for second harmonic generation.

O-K edge XANES spectroscopy evidences structural modification induced by thermal poling treatment in surfaces of bulk Herasil silica glass presenting second harmonic generation. Considering model silicon dioxide clusters, calculations based on full multiple scattering approach have been performed in order to explain accurately the differences observed on XANES spectra at different stage of the poling treatment. These structural modifications on extreme surface affect both network and defects by breaking Si-O-Si bridging bonds. Despite of the formation of bridging bond occurring during the thermal depoling -which erases the SHG inside the glass-, the initial structure of the unpoled sample is not reproduced.

Planar waveguides formed by Ag+-Na+ ion exchange in nonlinear optical glasses: diffusion and optical properties.

All-optical communication systems are the subject of intense research related to the integration of nonlinear optical materials. In sodiocalcic borophosphate glasses that contain niobium oxide and exhibit high nonlinear optical indices, planar waveguides have been formed by a Ag(+)-Na(+) ion-exchange technique. WKB analysis has been used to characterize the diffusion profiles of silver ions exchanged in glass substrate samples chemically by an electron microprobe technique and optically by an M-line technique. These methods permit the Ag(+) penetration depth and diffusion profile shape and index profiles to be determined. The results are analyzed and discussed in relation to Ca(2+) concentration and exchange conditions in glasses. The Ag(+) diffusion in these glasses can be almost entirely controlled for index-profile engineering.

Glycerol's influence on the oxidized insulin B-chain conformation in relation to the selectivity variation of subtilisin: an nuclear magnetic resonance and simulated annealing study.

Glycerol, employed to mimic biological media with restricted water activity, has been shown to modify the activity of subtilisin BPN', an endopeptidase, towards the oxidized insulin B-chain, a well-studied substrate (FEBS Lett., 279 (1991) 123-131). Without minimizing the role of the microenvironment on the enzyme, we have studied the effect of glycerol addition on the structure of the enzyme substrate by homonuclear NMR spectroscopy and simulated annealing. Our results show that, in water, the oxidized insulin B-chain tertiary structure loses its central helix (residues B9-B19) and presents a folded structure with a flexible turn (residues B18-B24) in the beta-turn region of the insulin B-chain; whereas, in glycerol, the peptide is more rigid and is not folded. Moreover, in our experimental conditions, glycerol favors beta-strand secondary structure formation. Following these results, hypotheses about the differences observed in enzymatic activity on this substrate in glycerol have been postulated.