Shivaji University

About: Shivaji University is a education organization based out in Kolhāpur, Maharashtra, India. It is known for research contribution in the topics: Thin film & Scanning electron microscope. The organization has 3078 authors who have published 5295 publications receiving 115397 citations.

Photocatalytic activity of sea water using TiO2 catalyst under solar light

Abstract: Wastewater is generally released into the rivers and streams in developing countries. Industrial wastewater usually contains highly toxic pollutants, cyanides, chlorinated compounds. Ultraviolet (UV) radiation from sunlight also decomposes organic compounds by oxidation process. However, the process is less effective due to large amount of toxic effluent entering in the main stream of water. The solar radiation can effectively be applied to accelerate the process by using suitable catalyst for economically cleaning the water sources. This paper describes the photocatalytic degradation of the sea water using novel approach of photoelectrochemical (PEC) reactor module consisting of nine photoelectrochemical cells equipped with spray deposited TiO₂ catalysts under solar light. The resulted water samples were studied for physicochemical and bacteriological analysis. The complete mineralization of degraded sample was confirmed by total organic carbon (TOC) analysis, COD measurement and estimation of the formation of inorganic ions such as NH₄(+), NO₃⁻, Cl⁻ and SO²⁻₄. Microbiological examinations are performed to determine the bacterial analysis. This implies that photoelectrocatalysis could be a promising way for improving water quality in developing countries with low cost and clean energy reliable resource.

Conformational Preferences of Modified Nucleoside N(4)-Acetylcytidine, ac4C Occur at “Wobble” 34th Position in the Anticodon Loop of tRNA

Abstract: Conformational preferences of modified nucleoside, N(4)-acetylcytidine, ac4C have been investigated using quantum chemical semi-empirical RM1 method. Automated geometry optimization using PM3 method along with ab initio methods HF SCF (6-31G**), and density functional theory (DFT; B3LYP/6-31G**) have also been made to compare the salient features. The most stable conformation of N(4)-acetyl group of ac4C prefers “proximal” orientation. This conformation is stabilized by intramolecular hydrogen bonding between O(7)···HC(5), O(2)···HC2′, and O4′···HC(6). The “proximal” conformation of N(4)-acetyl group has also been observed in another conformational study of anticodon loop of E. coli elongator tRNAMet. The solvent accessible surface area (SASA) calculations revealed the role of ac4C in anticodon loop. The explicit molecular dynamics simulation study also shows the “proximal” orientation of N(4)-acetyl group. The predicted “proximal” conformation would allow ac4C to interact with third base of codon AUG/AUA whereas the ‘distal’ orientation of N(4)-acetyl cytidine side-chain prevents such interactions. Single point energy calculation studies of various models of anticodon–codon bases revealed that the models ac4C(34)(Proximal):G3, and ac4C(34)(Proximal):A3 are energetically more stable as compared to models ac4C(34)(Distal):G3, and ac4C(34)(Distal):A3, respectively. MEPs calculations showed the unique potential tunnels between the hydrogen bond donor–acceptor atoms of ac4C(34)(Proximal):G3/A3 base pairs suggesting role of ac4C in recognition of third letter of codons AUG/AUA. The “distal” conformation of ac4C might prevent misreading of AUA codon. Hence, this study could be useful to understand the role of ac4C in the tertiary structure folding of tRNA as well as in the proper recognition of codons during protein biosynthesis process.