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A. Senthilkumar
Researcher at VIT University
Publications - 12
Citations - 234
A. Senthilkumar is an academic researcher from VIT University. The author has contributed to research in topics: Adsorption & Chemistry. The author has an hindex of 5, co-authored 5 publications receiving 176 citations.
Papers
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Journal ArticleDOI
Effects of oxygen enriched combustion on pollution and performance characteristics of a diesel engine
P. Baskar,A. Senthilkumar +1 more
TL;DR: In this paper, an experimental test was conducted on a single cylinder direct injection diesel engine to study the impact of oxygen enrichment on pollution and performance parameters by increasing the oxygen concentration of intake air from 21 to 27% by volume.
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Effect of Fe doping on the electrochemical capacitor behavior of MnO2 nanocrystals
TL;DR: In this paper, the influence of Fe doping on the capacitance behavior of MnO2 nanoparticles synthesized by chemical precipitation was investigated, where the concentration of Fe was increased from 0.025 m to 0.125 m in steps of 0.25 m.
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Influence of Zn doping on the electrochemical capacitor behavior of MnO2 nanocrystals
TL;DR: In this paper, a simple chemical precipitation method for the preparation of bare and different levels of Zn doped MnO2 nanoparticles as electrodes for supercapacitors was suggested.
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Pulsed current and dual pulse gas metal arc welding of grade AISI: 310S austenitic stainless steel
TL;DR: In this paper, the transverse shrinkage, mechanical and metallurgical properties of AISI: 310S ASS weld joints prepared by P-GMAW and DP GMAW processes were investigated.
Journal ArticleDOI
Computational analysis of deleterious missense mutations in aspartoacylase that cause Canavan's disease.
K. Sreevishnupriya,P. Chandrasekaran,A. Senthilkumar,Rao Sethumadhavan,V. Shanthi,P. Daisy,J. Nisha,K. Ramanathan,R. Rajasekaran +8 more
TL;DR: The present study showed that the majority of the substrate-binding amino acids in those 15 mutants displayed loss of flexibility, which could be the theoretical explanation of decreased binding affinity between the mutant aspartoacylases and NAA.