Application of Innovative Cost effective flow resistivity measurement system for Acoustic Performance Analysis of Natural fibers

In design of the interior of car, workplace and companies, acoustic material plays very important role. To attenuate unwanted noise, passive noise control technique using acoustic material is used extensively. The non-biodegradable synthetic acoustic material, which are used nowadays cause environmental pollution. This environmental pollution motivates researchers to find eco-friendly and sustainable acoustic materials as an alternative sound absorber. Research is going on to find new acoustic materials for many industrial and domestic applications. The value of sound absorption coefficient has correlation with frequency of sound. Hence, it would be very helpful if the characteristic acoustic properties of these materials are known prior using them for a particular application. This paper presents the utilization of new flow resistivity measurement set up. This flow resistivity set up is developed as per ASTM C522-03 standard. Delany-Bazley model can be used to predict sound absorption coefficient using flow resistivity values. The numerical analysis using MATLAB program based on Delany-Bazley models is made to determine sound absorption coefficient of material prepared from natural fibers of sugarcane waste, wheat straw and PU foam, Glass wool. The sound absorption coefficients of all four materials are also obtained by experimental investigation using impedance tube as per ASTM E 1050 standard. Comparisons of the experimental and the numerical results confirm that the sound absorption coefficients of all material are well corroborated

Characterization of NiO-Al2O3 composite and its conductivity in biogas for solid oxide fuel cell

NiO-Al O nanocomposite has been synthesized by mixing combustion synthesized powders. The nanocomposite is an effective anode/anode functional layer for intermediate temperature solid oxide fuel cells. The TEM of NiO and Al O revealed spherical particles of 30 nm and platelets of 70 nm, respectively. The XRD analysis of NiO-Al O composite sintered at 900 °C showed presence of cubic NiO and rhombohedral α-Al O which were chemically stable. However, above 1200 °C NiAl O started to appear. The conductivity of NiO-Al O was the highest in hydrogen (4.3 × 10 S/cm at 600 °C). In biogas, the conductivity was 3.2 × 10 S/cm with the activation energy of 0.67 eV. The stability of the composite in biogas was also examined

S-Benzyl­thio­uronium 3-nitro­benzene­sulfonate

In the title compound, C8H11N2S+·C6H4NO5S−, the asymmetric unit is composed of two crystallographically independent S-benzyl­thio­uronium cations and two independent nitro­benzene­sulfonate anions. An intra­molecular hydrogen bond generates an S(5)S(5) ring motif. The crystal packing is stabilized by intra­molecular C—H⋯O and inter­molecular C—H⋯O, N—H⋯O and N—H⋯S hydrogen bonds which, along with short S⋯O [3.034 (2) Å] and N⋯O [2.796 (3) Å] contacts, form a two-dimensional network parallel to the ab plane

(E)-3-(4-Methyl­phen­yl)-1-(4-nitro­phenyl)prop-2-en-1-one

The asymmetric unit of the title compound, C16H13NO3, contains two independent mol­ecules related approximately by a pseudo-twofold rotation axis. The dihedral angle between the nitro­benzene and methyl­phenyl rings is 42.18 (6)° in one mol­ecule and 12.97 (6)° in the other. In both mol­ecules, the nitro group is slightly twisted away from the attached benzene ring. In the crystal structure, the mol­ecules are stacked along the b axis and are linked via C—H⋯O and C—H⋯π inter­actions

2,5-Dimethoxy­benzaldehyde thio­semicarbazone

In the title mol­ecule, C10H13N3O2S, the dihedral angle between benzene and –N—C(=S)—N—N=C– planes is 9.20 (6)°. The two meth­oxy groups are coplanar with the benzene ring [C—O—C—C torsion angles of −2.31 (18) and −6.45 (17)°]. In the crystal structure, mol­ecules are linked by inter­molecular N—H⋯S, N—H⋯O and C—H⋯O hydrogen bonds, forming a three-dimensional network

(E)-3-(2-Chloro­phen­yl)-1-(4-chloro­phen­yl)prop-2-en-1-one

The title compound, C15H10Cl2O, adopts an E configuration with respect to the C=C bond of the propenone unit. The dihedral angle between the two benzene rings is 32.4 (1)°. Intra­molecular C—H⋯O and C—H⋯Cl hydrogen bonds generate an S(5)S(5)S(5) motif. In addition, the crystal structure is stabilized by weak inter­molecular C—H⋯O hydrogen bonds

3-Hydr­oxy-4-methoxy­benzaldehyde thio­semicarbazone hemihydrate

The asymmetric unit of the title compound, C9H11N3O2S·0.5H2O, comprises two crystallograpically independent thio­semicarbazone mol­ecules (A and B) and a water mol­ecule of crystallization. In each of the thio­semicarbazone mol­ecules, intra­molecular O—H⋯O and N—H⋯N hydrogen bonds form five-membered rings, producing S(5) ring motifs. Inter­molecular O—H⋯S and N—H⋯O inter­actions between mol­ecule B and the water mol­ecule form a six-membered ring, producing an R 2 2(6) ring motif. Inter­molecular N—H⋯S hydrogen bonds form dimers involving pairs of both A and B mol­ecules, which form R 2 2(8) ring motifs. The angles between the aromatic ring and thio­urea unit in the two mol­ecules are 0.80 (6) and 3.28 (5)°, which proves that each mol­ecule is fairly planar. The crystal structure is stabilized by inter­molecular O—H⋯S (×2), O—H⋯O, N—H⋯S (×2) and N—H⋯O (×2) hydrogen bonds and C—H⋯O (×2) contacts to form a three-dimensional network

m^6A RNA methylation promotes XIST-mediated transcriptional repression

The long non-coding RNA X-inactive specific transcript (XIST) mediates the transcriptional silencing of genes on the X chromosome. Here we show that, in human cells, XIST is highly methylated with at least 78 N^6-methyladenosine (m^6A) residues—a reversible base modification of unknown function in long non-coding RNAs. We show that m^6A formation in XIST, as well as in cellular mRNAs, is mediated by RNA-binding motif protein 15 (RBM15) and its paralogue RBM15B, which bind the m^6A-methylation complex and recruit it to specific sites in RNA. This results in the methylation of adenosine nucleotides in adjacent m^6A consensus motifs. Furthermore, we show that knockdown of RBM15 and RBM15B, or knockdown of methyltransferase like 3 (METTL3), an m^6A methyltransferase, impairs XIST-mediated gene silencing. A systematic comparison of m^6A-binding proteins shows that YTH domain containing 1 (YTHDC1) preferentially recognizes m^6A residues on XIST and is required for XIST function. Additionally, artificial tethering of YTHDC1 to XIST rescues XIST-mediated silencing upon loss of m^6A. These data reveal a pathway of m^6A formation and recognition required for XIST-mediated transcriptional repression

Generation, annotation, and analysis of ESTs from midgut tissue of adult female Anopheles stephensi mosquitoes

<p>Abstract</p> <p>Background</p> <p>Malaria is a tropical disease caused by protozoan parasite, <it>Plasmodium</it>, which is transmitted to humans by various species of female anopheline mosquitoes. <it>Anopheles stephensi </it>is one such major malaria vector in urban parts of the Indian subcontinent. Unlike <it>Anopheles gambiae</it>, an African malaria vector, transcriptome of <it>A. stephensi </it>midgut tissue is less explored. We have therefore carried out generation, annotation, and analysis of expressed sequence tags from sugar-fed and <it>Plasmodium yoelii </it>infected blood-fed (post 24 h) adult female <it>A. stephensi </it>midgut tissue.</p> <p>Results</p> <p>We obtained 7061 and 8306 ESTs from the sugar-fed and <it>P. yoelii </it>infected mosquito midgut tissue libraries, respectively. ESTs from the combined dataset formed 1319 contigs and 2627 singlets, totaling to 3946 unique transcripts. Putative functions were assigned to 1615 (40.9%) transcripts using BLASTX against UniProtKB database. Amongst unannotated transcripts, we identified 1513 putative novel transcripts and 818 potential untranslated regions (UTRs). Statistical comparison of annotated and unannotated ESTs from the two libraries identified 119 differentially regulated genes. Out of 3946 unique transcripts, only 1387 transcripts were mapped on the <it>A. gambiae </it>genome. These also included 189 novel transcripts, which were mapped to the unannotated regions of the genome. The EST data is available as ESTDB at <url>http://mycompdb.bioinfo-portal.cdac.in/cgi-bin/est/index.cgi</url>.</p> <p>Conclusion</p> <p>3946 unique transcripts were successfully identified from the adult female <it>A. stephensi </it>midgut tissue. These data can be used for microarray development for better understanding of vector-parasite relationship and to study differences or similarities with other malaria vectors. Mapping of putative novel transcripts from <it>A. stephensi </it>on the <it>A. gambiae </it>genome proved fruitful in identification and annotation of several genes. Failure of some novel transcripts to map on the <it>A. gambiae </it>genome indicates existence of substantial genomic dissimilarities between these two potent malaria vectors.</p

m^6A RNA methylation promotes XIST-mediated transcriptional repression

The long non-coding RNA X-inactive specific transcript (XIST) mediates the transcriptional silencing of genes on the X chromosome. Here we show that, in human cells, XIST is highly methylated with at least 78 N^6-methyladenosine (m^6A) residues—a reversible base modification of unknown function in long non-coding RNAs. We show that m^6A formation in XIST, as well as in cellular mRNAs, is mediated by RNA-binding motif protein 15 (RBM15) and its paralogue RBM15B, which bind the m^6A-methylation complex and recruit it to specific sites in RNA. This results in the methylation of adenosine nucleotides in adjacent m^6A consensus motifs. Furthermore, we show that knockdown of RBM15 and RBM15B, or knockdown of methyltransferase like 3 (METTL3), an m^6A methyltransferase, impairs XIST-mediated gene silencing. A systematic comparison of m^6A-binding proteins shows that YTH domain containing 1 (YTHDC1) preferentially recognizes m^6A residues on XIST and is required for XIST function. Additionally, artificial tethering of YTHDC1 to XIST rescues XIST-mediated silencing upon loss of m^6A. These data reveal a pathway of m^6A formation and recognition required for XIST-mediated transcriptional repression