36 resultados para Fundamental Domains


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We have studied the vertical transport and formation mechanisms of electric field domains in doped weakly-coupled GaAs/AlAs superlattices. Under hydrostatic pressure two kinds of sequential resonant tunneling are observed within the pressure range from 0 to 4.5 kbar. A transition from Gamma-Gamma to Gamma-X sequential resonant tunneling occurs at P-t approximate to 1.6 kbar. For P < P-t, the high electric field domain is formed by the Gamma-Gamma process, while for P > P-t it is preferentially formed by the Gamma-X process.

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Hydrostatic pressure measurements are used to investigate the formation mechanism of electric field domains in doped weakly-coupled GaAs/AlAs superlattices. For the first plateau-like region in the I-V curve, two kinds of sequential resonant tunnelling are observed. For P<2 kbar the high-field domain is formed by the Gamma-Gamma process, while for P>2 kbar the high-field domain is formed by the T-X process. For the second plateau-libe region, the high-field domain is attributed to Gamma-X sequential resonant tunnelling. (C) 1998 Elsevier Science B.V. All rights reserved.

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The structural and morphological evolution of mono-domains in thin films has been investigated for a series of liquid crystalline (LC) copolyethers. The copolyethers studied were synthesized by the reaction of 1-(4-hydroxy-4 ' -biphenylyl)-2-(4-hydroxyl-phenyl)propane (TPP) with 1,7-dibromoheptane and 1,11-undecane at different compositions (coTPPs-7/11). In contrast to the solution-cast thin films without annealing, which exhibit the isotropic homogeneous molecular orientation, mono-domains with a homeotropic alignment were found in coTPP-7/11(5/5) after the thin films were annealed in the high-temperature columnar phase (Phi '). Similar to the nucleation process in polymer crystallization, transmission electron microscopic observations show that small mono-domains appear in the initial stage of annealing, where molecules form a uniaxial in-plane chain orientation. With increasing annealing time, the molecular orientation gradually became tilted with respect to the substrate surface, and finally, a uniaxial homeotropic molecular orientation was achieved after a prolonged annealing time. The lateral size of mono-domains was found to increase continuously with annealing time and grew into a circular shape, indicating an isotropic lateral growth scheme which implies a hexagonal molecular packing proved by the electron diffraction experiments.

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Clip domain serine protease (cSP), characterized by conserved clip domains, is a new serine protease family identified mainly in arthropod, and plays important roles in development and immunity. In the present study, the full-length cDNA of a cSP (designated EscSP) was cloned from Chinese mitten crab Eriocheir sinensis by expressed sequence tags (ESTs) and PCR techniques. The 1380 bp EscSP cDNA contained a 1152 bp open reading frame (ORF) encoding a putative cSP of 383 amino acids, a 5'-untranslated region (UTR) of 54 bp, and a 3'-UTR of 174 bp. Multiple sequence alignment presented twelve conserved cysteine residues and a canonical catalytic triad (His(185), Asp(235) and Ser(332)) critical for the fundamental structure and function of EscSP. Two types of cSP domains, the clip domain and tryp_spc domain, were identified in the deduced amino acids sequence of EscSP. The conservation characteristics and similarities with previously known cSPs indicated that EscSP was a member of the large cSP family. The mRNA expression of EscSP in different tissues and the temporal expression in haemocytes challenged by Listonella anguillarum were measured by real-time RT-PCR. EscSP mRNA transcripts could be detected in all examined tissues, and were higher expressed in muscle than that in hepatopancreas. gill, gonad, haemocytes and heart. The EscSP mRNA expression in haemocytes was up-regulated after L anguillarum challenge and peaked at 2 h (4.96 fold, P < 0.05) and 12 h (9.90 fold, P < 0.05). Its expression pattern was similar to prophenoloxidase (EsproPO), one of the components of crab proPO system found in our previous report. These results implied that EscSP was involved in the processes of host-pathogen interaction probably as one of the proPO system members. (C) 2009 Elsevier Ltd. All rights reserved.

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C-type lectins are a superfamily of carbohydrate-recognition proteins which play crucial roles in the innate immunity. In this study, the gene of a C-type lectin with multiple carbohydrate-recognition domains (CRDs) from scallop Chlamys farreri (designated as Cflec-3) was cloned by rapid amplification of cDNA ends (RACE) approach based on expression sequence tag (EST) analysis. The full-length cDNA of Cflec-3 was of 2256 bp. The open reading frame encoded a polypeptide of 516 amino acids, including a signal sequence and three CRDs. The deduced amino acid sequence of Cflec-3 showed high similarity to members of C-type lectin superfamily. By fluorescent quantitative real-time PCR, the Cflec-3 mRNA was mainly detected in hepatopancreas, adductor, mantle, and marginally in gill, gonad and hemocytes of healthy scallops. After scallops were challenged by Listonella anguillarum, the mRNA level of Cflec-3 in hemocytes was up-regulated and was significantly higher than that of blank at 8 h and 12 h post-challenge. The function of Cflec-3 was investigated by recombination and expression of the cDNA fragment encoding its mature peptide in Escherichia coli BL21 (DE3)-pLysS. The recombined Cflec-3 (rCflec-3) agglutinated Gram-negative bacteria Pseudomonas stutzeri. The agglutinating activity was calcium-dependent and could be inhibited by D-mannose. These results collectively suggested that Cflec-3 was involved in the immune response against microbe infection and contributed to nonself-recognition and clearance of bacterial pathogens in scallop. (C) 2009 Elsevier Ltd. All rights reserved.