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Amit Kumar Mandal

Researcher at St. John's University

Publications -  64
Citations -  892

Amit Kumar Mandal is an academic researcher from St. John's University. The author has contributed to research in topics: Hemoglobin & Hemoglobin variants. The author has an hindex of 15, co-authored 63 publications receiving 777 citations. Previous affiliations of Amit Kumar Mandal include Indian Institute of Science Education and Research, Kolkata & Bose Institute.

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Ionic liquid integrated multiwalled carbon nanotube in a poly(vinylidene fluoride) matrix: formation of a piezoelectric β-polymorph with significant reinforcement and conductivity improvement.

TL;DR: A differential scanning calorimetry (DSC) study shows that the MWNT-ILs are an efficient nucleating agent for PVDF crystallization preferentially nucleating the β form due to its dipolar interactions with PVDF.
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Solvation Dynamics of a Probe Covalently Bound to a Protein and in an AOT Microemulsion: 4-(N-Bromoacetylamino)-Phthalimide

TL;DR: In this article, the photophysics of the probe 4-(N-bromoacetylamino)-phthalimide (I) is dramatically different from that of the parent compound, 4-aminophthalimide.
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Quantitation and characterization of glutathionyl haemoglobin as an oxidative stress marker in chronic renal failure by mass spectrometry

TL;DR: Glutathionyl haemoglobin can serve as a clinical marker of oxidative stress in chronic debilitating therapies like RRT, and mass spectrometry provides a reliable analytical tool for quantitation and residue level characterization of different post-translational modifications of haenoglobin.
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Diffusion of Organic Dyes in Immobilized and Free Catanionic Vesicles

TL;DR: Fluorescence correlation spectroscopy has been used to study the motion of fluorescent dyes in a giant catanionic vesicle comprised of the surfactant sodium dodecyl sulfate (SDS) and dodecymethyl ammonium bromide (DTAB).
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Glutamate counteracts the denaturing effect of urea through its effect on the denatured state

TL;DR: D-Glutamate has a similar effect on the equilibrium denaturation of glutaminyl-tRNA synthetase, indicating that the effect of l-glutamate may not be due to substrate-like binding to the native state, and Dramatic increase of coefficient of urea concentration dependence values of both the transitions in the presence of glutamate suggests destabilization and increased solvent exposure of the denatured states.