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Tejbal Singh

Researcher at All India Institute of Medical Sciences

Publications -  57
Citations -  696

Tejbal Singh is an academic researcher from All India Institute of Medical Sciences. The author has contributed to research in topics: Hydrogen bond & Active site. The author has an hindex of 12, co-authored 50 publications receiving 616 citations.

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First structural evidence of a specific inhibition of phospholipase A2 by alpha-tocopherol (vitamin E) and its implications in inflammation: crystal structure of the complex formed between phospholipase A2 and alpha-tocopherol at 1.8 A resolution.

TL;DR: This is the first structural evidence of alpha-tocopherol (alpha-TP) as a possible candidate against inflammation, as it inhibits phospholipase A2 specifically and effectively, resulting in the formation of a stable complex.
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A hybrid Taguchi-artificial neural network approach to predict surface roughness during electric discharge machining of titanium alloys

TL;DR: In this paper, Artificial neural network coupled with Taguchi approach was applied for optimization and prediction of surface roughness, the experimental results and the predicted results showed good agreement and SEM was used to investigate the surface integrity, the results showed that high discharge energy caused surface defects such as cracks, craters, micro pores, pin holes, residual stresses and debris.
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Enhancement of enzyme activity through three-phase partitioning: crystal structure of a modified serine proteinase at 1.5 Å resolution

TL;DR: The structure of the TPP-treated proteinase K appears that the protein exists in an excited state which might be helping the enzyme to function more rapidly than the original enzyme in aqueous media.
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Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma

TL;DR: This is the first report on the formation of a complex between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) and the structure shows that the beta-structure of PIP is ideally aligned with the alpha1-alpha2 domains of ZAG to form a long interface between two proteins.
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Specific binding of non-steroidal anti-inflammatory drugs (NSAIDs) to phospholipase A2: structure of the complex formed between phospholipase A2 and diclofenac at 2.7 A resolution.

TL;DR: The detailed three-dimensional structure of a complex formed between a group IIA PLA2 from Daboia russelli pulchella and 2-[(2,6-dichlorophenyl)amino]benzeneacetic acid has been determined and showed that diclofenac occupies a very favourable position in the centre of the substrate-binding hydrophobic channel that allows a number of intermolecular interactions.