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Exploring novel hypergolic fuels for modern space propulsion is highly desired. However, the analysis and understanding of the structure and hypergolic performance at the molecular level are still insufficient. To understand the factors that dictate hypergolicity, we conducted a comparative study on a series of metal-organic frameworks (MOFs) characterized by the same topology but with varied ligand structures. The ignition delay (ID) time trend was found to be imidazoletriazoletetrazole, and the rapid ID time was 8 ms. By combining experimental studies and density functional theory (DFT) calculations, we found that propargyl and cyanoborohydride groups that functioned as dual hypergolic triggers contributed to the hypergolicity, and a distinct electronic structure was detrimental to ID time. The structure-performance relationships presented herein can potentially provide some fundamental insights into the field of developing high-performance hypergolic fuels.

[Ni(hmp)(MeOH)Br]4 ⋅ 2H2O has been prepared by the reaction of 2-hydroxymethylpyridine with NiBr2 ⋅ 3H2O and characterized by IR, elemental analysis, powder X-ray diffraction, thermogravimetric analyses, magnetic measurements, and single crystal X-ray diffraction. The crystal structure shows two independent [Ni(hmp)(MeOH)Br]4 molecules in the asymmetric unit and [Ni4O4]4+ cubane-type cores. Each octahedral Ni(II) is bridged by four μ3-CH2O − fragments from four hmp − ligands. Magnetic studies show that ferromagnetic coupling gives an S = 4 ground state with significant magnetoanisotropy, and the parameters are J 1 = 8.56, J 2 = 2.28, D = −0.65 cm−1, and g ≈ 2.13.

A novel bilayered coordination polymer with nanoporous channels [Ni3(bix)3(PTCO)2 (H2O)4·6H2O]n (1) has been synthesized and the permanent porosity of (1) is confirmed by N2 adsorption isotherm measurement.

Three novel 3D metal–organic frameworks, [Co2(butca)(o-bix)2·8H2O]n (1), [Co2(butca)(m-bix)2·2H2O]n (2) and [Co2(butca)(p-bix)2·3H2O]n (3) (butca = 1,2,3,4-butane-tetracarboxylic acid; o-bix = 1,2-bis(imidazol-1-ylmethyl)-benzene; m-bix = 1,3-bis(imidazol-1-ylmethyl)-benzene; and p-bix = 1,4-bis(imidazol-1-ylmethyl)-benzene), have been successfully synthesized from a 2D layer compound [Co2(butca)(H2O)5·2H2O]n (0) employing a three isomer pillars insertion reaction, and their structures were determined by single-crystal X-ray diffraction studies. Complexes 1 and 2 are isostructural. Interestingly, there exist metal-bix double-helical chains in these two 3D frameworks, which are arranged left- and right-handed alternately. Different from 1 and 2 which have only one coordination model, Co atoms in 3 have two types of different coordination enviroments. The Co1 ions are exclusively bridged by cis-bix ligands to give one 26-number ring through spontaneous resolution. At the same time, the Co2 ions are wholely connected with tran-bix ligands to form a 1-D zigzag chain. Moreover, the relationship between a 2D layer structure and 3D metal–organic frameworks based on the pillared-layer motifs is discussed. This work has significant potential for the study of crystal engineering of transition metal coordination networks.

The AP2/EREBP transcription factors play important roles in plant development and in the responses of plants to biotic and abiotic stresses. All members of the EREBP subfamily described to date are from dicotyledonous plants. In this paper, we describe the cloning and characterization of a rice gene, OsEBP-89, encoding a protein 326 amino acids long with a typical EREBP domain; this is the first report of an EREBP transcription factor in a monocotyledonous plant. Except for the EREBP domain, the OsEBP-89 protein does not have substantial sequence similarities to other members of the subfamily. The DNA-binding activity of the EREBP domain was confirmed by electrophoretic mobility-shift assays. An activation domain rich in acidic amino acids was identified by using a yeast one-hybrid system. Two putative nuclear-localization signals were also identified. The results of northern blot hybridization experiments showed that the transcript of the OsEBP-89 gene accumulates primarily in immature seeds, roots, and leaves (low levels). More detailed information about the pattern of OsEBP-89gene expression was obtained by histochemical studies of transgenic rice plants carrying an OsEBP-89 5′/GUS reporter gene. The reporter gene was expressed in the endosperm starting at 7 days after pollination and in the intercalary meristem of plants. Expression of OsEBP-89was induced in roots of rice seedlings by treatment with ACC, NaCl, or 2,4-D. Two cis-acting elements, an endosperm motif and a primary PERE, are present upstream of the OsEBP-89 coding region and may be involved in regulating its expression. Collectively, these results suggest that the OsEBP-89gene is a new member of the EREBP subfamily and may be involved in ethylene-dependent seed maturation and shoot development of rice.

We have previously reported that three distinct patterns of waxy (Wx) gene transcript accumulation were present in 31 rice cultivars. The cultivars with high amylose content (group I) contain a 2.3 kb mature Wx mRNA, cultivars with intermediate amylose content (group II) produce both a 3.3 kb Wx pre-mRNA, which contains intron 1, and the 2.3 kb Wx mature mRNA, and cultivars with no amylose (group III) accumulate only the 3.3 kb Wx pre-mRNA. Analyses of the cDNAs reveals that four splice donor sites and three splice acceptor sites in intron 1 give rise to six splicing patterns in 2.3 kb Wx mRNA of group II cultivars. In addition, aberrant intron 1 excision causes either deletion of 4 or 5 nucleotides, or addition of 7 and 13 nucleotides at the junction of exon 1 and exon 2 of the 2.3 kb mRNA. In contrast, only one normal splicing pattern (one splice donor site and one splice acceptor site) was found in the 2.3 kb mRNA of group I cultivars. Nucleotide sequences of the Wx intron 1 in group I and group II cultivars differ by 16 individual bases. We suggest that these deletions or additions contribute to inefficient splicing of intron 1 from the 3.3 kb Wx pre-mRNA, as well as an aberrant splicing of the Wx intron 1 to produce the 2.3 kb mRNA with a heterogeneous 5' untranslated region (5'-UTR). As a consequence, the total amount of translatable Wx mRNA, and therefore the Wx protein and amylose content, are reduced in the group II cultivars compared with the group I cultivars.

To investigate the protective effect and mechanism of curcumin against ActD/TNF-α-induced synergistically apoptosis in PC12 cells.MTT assay was used to evaluate the optimal concentration of drugs; Hoechst 33258 fluorescent staining to observe apoptosis of PC12 cells, JC-1 was used to detect the mitochondrial membrane potential (MMP), real-time PCR was used to detect the expression of two apoptotic genes: Bcl-1 and Bax.ActD/TNF-α can synergistically reduce viability of PC12 cells(P0.05), increase the number of cells with pyknosis and karyorrhexis, increase apoptotic rate of cells (P0.05), decrease MMP in cells, and downregulate expression of Bcl-2(P0.05). After treating with curcumin(5 μmol/L), survival of PC12 cells was increased(P0.05), the number of cells with pyknosis and karyorrhexis was reduced, MMP and expression of Bcl-2 were increased(P0.05).Curcumin can resist the ActD/TNF-α-induced synergistically apoptosis in PC12 cells, the mechanisms of which may be related to an increase in MMP and Bcl-2 expression.

In order to study the spectral characteristics and color-genetic mechanism of the scheelite with orange color found in scheelite-tin-beryl (W-Sn-Be) deposits in Xuebaoding, four groups of scheelite were investigated by means of EMPA, IR, LRM and XRD. The scheelite samples were tested by XRD and IR in order to reveal if there are other minerals intermingled with scheelite. Meanwhile, the structure, the structure water and the crystal water were studied through infrared spectra. The absorption bands and peaks of infrared and Raman spectra were assigned. Finally, it seems that there is no distinct color difference between scheelite from Xue baoding and those from other places. So, it is conceived that the color causing may correlate with the minor crystal structure, trace element or REE in the crystal.

The AP2/EREBP transcription factors play important roles in plant development and in the responses of plants to biotic and abiotic stresses. All members of the EREBP subfamily described to date are from dicotyledonous plants. In this paper, we describe the cloning and characterization of a rice gene, OsEBP-89, encoding a protein 326 amino acids long with a typical EREBP domain; this is the first report of an EREBP transcription factor in a monocotyledonous plant. Except for the EREBP domain, the OsEBP-89 protein does not have substantial sequence similarities to other members of the subfamily. The DNA-binding activity of the EREBP domain was confirmed by electrophoretic mobility-shift assays. An activation domain rich in acidic amino acids was identified by using a yeast one-hybrid system. Two putative nuclear-localization signals were also identified. The results of northern blot hybridization experiments showed that the transcript of the OsEBP-89 gene accumulates primarily in immature seeds, roots, and leaves (low levels). More detailed information about the pattern of OsEBP-89 gene expression was obtained by histochemical studies of transgenic rice plants carrying an OsEBP-89 5'/GUS reporter gene. The reporter gene was expressed in the endosperm starting at 7 days after pollination and in the intercalary meristem of plants. Expression of OsEBP-89 was induced in roots of rice seedlings by treatment with ACC, NaCl, or 2,4-D. Two cis-acting elements, an endosperm motif and a primary PERE, are present upstream of the OsEBP-89 coding region and may be involved in regulating its expression. Collectively, these results suggest that the OsEBP-89 gene is a new member of the EREBP subfamily and may be involved in ethylene-dependent seed maturation and shoot development of rice.

Cis-acting elements containing CCAAT core sequence are located in 5′ upstream regions of numerous eukaryotic genes. CCAAT-binding factors interact with thesecis acting elements as heteromeric complex and therefore control the gene transcription. CCAAT binding factors contain at least three subunits and each subunit alone cannot bind to CCAAT box. The cloning of a rice cDNA called RAPB which homologizes to yeast HAP2 (one of the subunits in CCAAT-binding factors) using yeast one-hybrid system and functional complementation approaches is reported. The analytic results indicate that the deduced amino acid sequence in the C terminal of RAPB also contains the functional domain of 60 amino acids highly homologous with yeast HAP2, whereas the deduced amino acids in N terminal region differs significantly, and no Gln-rich region is found in the RAPB protein as in HAP2. The Southern blotting analysis demonstrates that only one copy of RAPB gene exists in rice genome.

DNase I footprints and affinity measurements showed that the C-terminal arm of Xenopus transcription factor IIIA interacts differently with different Xenopus 5S DNAs, forming three distinct types of transcription factor IIIA-5S DNA complexes: a somatic type, a major-oocyte (and pseudogene) type, and a trace-oocyte type. Site-directed mutagenesis on the major-oocyte 5S gene revealed that somatic-type changes at positions 53, 55, and 56 changed the structure of the transcription factor IIIA-5S DNA complex from major-oocyte to somatic, and a single trace-oocyte change at position 56 caused the change from major-oocyte to trace-oocyte complex. We further show that the somatic-type changes are accompanied by a marked enhancement in the rate of 5S RNA transcription, and we discuss the possible biological relevance of these findings.

7S particles from Xenopus oocytes were completely dissociated under non-reducing conditions. Studies using glycerol gradient centrifugation show that unlike the native 7S particle in which 5S RNA and TFIIIA co-sedimented in a fairly sharp peak, the RNA from the denatured 7S sedimented at the position corresponding to the 5S RNA and the TFIIIA sedimented as a wide peak between 6S and 12S. Thioredoxin from E. coli can catalyze the reactivation of the TFIIIA as measured by its ability to reform the 7S particle. The rate of reactivation with thioredoxin was significantly greater than with dithiothreitol. Oxidized thioredoxin was unable to reactivate TFIIIA. Pure TFIIIA can be inactivated and subsequently reactivated in the same way by formation of a cross-linked structure via intermolecular disulfide bridges.