Investigation of structural and electrical properties of electrolyte LaGaO for solid oxide fuel cell.

Context: Electrochemical devices such as solid oxide fuel cells (SOFCs) allow the direct transformation of fuel's chemical energy into electrical power. Even though YSZ electrolyte-based conventional SOFCs are widely used in both laboratories and on a commercial scale, developing alternative ion-conducting electrolytes is crucial for enhancing SOFC performance at lower operating temperatures. In this work, we conducted a thorough computational analysis on the characteristics of Sr- and Mg-doped superior oxide ion conductors.

Study on the electronics and structural properties of transition metal-doped LaMoO.

Context: LaMoO is a potential electrolyte material for SOFC due to its higher oxygen conduction at high temperatures. However, LaMoO suffers from detrimental phase transition at high temperature from monoclinic α to cubic β phase. This phase transition can be prevented by lowering the temperature.

Population genetic structure and geographic differentiation in butter catfish, Ompok bimaculatus, from Indian waters inferred by cytochrome b mitochondrial gene.

Documentation of genetic differentiation among the populations of a species can provide useful information that has roles in conservation, breeding, and management plans. In the present study, we examined the genetic structure and phylogenetic relationships among the 149 individuals of Ompok bimaculatus belonging to 24 populations, collected from Indian waters, using cytochrome b gene. The combined analyses of data suggested that the Indian O.

Inducing toxicity by introducing a leucine-zipper-like motif in frog antimicrobial peptide, magainin 2.

Cytotoxicity, a major obstacle in therapeutic application of antimicrobial peptides, is controlled by leucine-zipper-like sequences in melittin and other naturally occurring antimicrobial peptides. Magainin 2 shows significantly lower cytotoxicity than many naturally occurring antimicrobial peptides and lacks this structural element. To investigate the consequences of introducing a leucine zipper sequence in magainin 2, a novel analogue (Mag-mut) was designed by rearranging only the positions of its hydrophobic amino acids to include this structural element.

A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: plausible implications in the toxic activity of the protein.

Hemolysin E (HlyE), a pore-forming protein-toxin and a potential virulence factor of Escherichia coli, exhibits cytotoxic activity to mammalian cells. However, very little is known about how the different individual segments contribute in the toxic activity of the protein. Toward this end, the role of a 33-residue segment comprising the amino acid region 88 to 120, which contains the putative transmembrane domain in the tail region of HlyE has been addressed in the toxic activity of the protein-toxin by characterizing the related wild type and mutant peptides and the whole protein.

Inhibition of lytic activity of Escherichia coli toxin hemolysin E against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism.

To investigate as to whether a peptide derived from hemolysin E (HlyE) can inhibit the cytotoxic activity of this protein or not, several peptides were examined for their efficacy to inhibit the lytic activity of the protein against human red blood cells (hRBCs). It was found that a wild-type peptide, H-205, derived from an amphipathic leucine zipper motif, located in the amino acid region 205-234, inhibited the lytic activity of hemolysin E against hRBCs. To understand the basis of this inhibition, several functional and structural studies were performed.