986 resultados para <1.75 phi
Resumo:
Top-illuminated metamorphic InGaAs p-i-n photodetectors (PDs) with 50% cut-off wavelength of 1.75 mu m at room temperature are fabricated on GaAs substrates. The PDs are grown by a solid-source molecular beam epitaxy system. The large lattice mismatch strain is accommodated by growth of a linearly graded buffer layer to create a high quality virtual InP substrate indium content in the metamorphic buffer layer linearly changes from 2% to 60%. The dark current densities are typically 5 x 10(-6) A/cm(2) at 0 V bias and 2.24 x 10(-4) A/cm(2) at a reverse bias of 5 V. At a wavelength of 1.55 mu m, the PDs have an optical responsivity of 0.48 A/W, a linear photoresponse up to 5 mW optical power at -4 V bias. The measured -3 dB bandwidth of a 32 mu m diameter device is 7 GHz. This work proves that InGaAs buffer layers grown by solid source MBE are promising candidates for GaAs-based long wavelength devices.
Resumo:
Ce ms. a appartenu à l'avocat parisien Antoine Loisel (1536-1617) (signature au f. 1), grand-père de Claude Joly, chantre de Notre-Dame, qui légua les mss. dont il avait hérité de son grand-père au chapitre de Notre-Dame de Paris en 1680. Notre-Dame.
Resumo:
Commençant par : « Estant couché soubz ung myrthe plaisant, Et maintz chasteaulx en Espaigne faisant... » et finissant par : « Sans parage ou riens n'est nect, Moulu d'un groz Moulinet. Fin de la complaincte de Grece, composée par le dict Molinet » .
Resumo:
The results of geological mapping, chemical analysis and radiometric dating of metabasic rocks of Betara Formation, and mapping and dating of those present in the Betara basement nucleus together with mylonitic granodiorite and syenogranite are reported here. U-Pb analysis of bulk zircon fractions from the metabasic rocks of the basement nucleus yielded a Statherian age of 1790 +/- 22 Ma, while the metabasic rocks from the upper part of the Betara Formation yielded a Calymmian age between 1500 and 1450 Ma. This age is a minimum for the deposition of the Betara Formation. The older metabasic rocks are associated with post-tectonic, possibly anorogenic syenogranite, while the younger ones are gabbro or very porphyritic ankaramite whose REE patterns are consistent with crystallization from an N-MORB parent magma. The observations and data point to the probable events associated with extensional processes of the end of Paleoproterozoic and early Mesoproterozoic. Similar registers of Statherian (1.80-1.75 Ga) and Calymmian (1.50-1.45 Ga) extensional events are recorded in other parts of the South American and African continents. The Neoproterozoic witnessed the formation and junction of the tectonic slices which formed the Apiai domain during the assemblage of western Gondwana. (C) 2010 International Association for Gondwana Research. Published by Elsevier B.V. All rights reserved.
Resumo:
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 +/- 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-lengthamino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 angstrom resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (beta alpha)(8) barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
Resumo:
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα) 8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors.