Vinod K. Aswal
Bhabha Atomic Research Centre
641 Papers
3.7K Citations
Vinod K. Aswal is an academic researcher from Bhabha Atomic Research Centre. The author has contributed to research in topics: Micelle & Small-angle neutron scattering. The author has an hindex of 46, co-authored 556 publications. Previous affiliations of Vinod K. Aswal include Paul Scherrer Institute & Indian Institute of Science.
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Papers
Aggregation and polymerization of PEG-Based macromonomers with methacryloyl group as the only hydrophobic segment
Souvik Maiti,P. R. Chatterji,C. K. Nisha,Sunkara V. Manorama,Vinod K. Aswal,Prem S. Goyal +5 more
- 15 Aug 2001
TL;DR: Aggregation behavior in aqueous solution of a series of poly (ethylene glycol) (PEG)-based macromonomers with methacryloyl group as the only hydrophobic segment has been investigated using surface tension, steady-state and time-resolved fluorescence spectroscopy, and small-angle neutron scattering techniques.
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Solubilization and location of phenol and benzene in a nonlinear amphiphilic EO–PO block copolymer micelles: 1H NMR and SANS studies
TL;DR: In this paper, the aqueous solution behavior of a poly(ethylene oxide)-poly(propylene oxide), PEO-PPO, star block copolymer Tetronic® T904 with solubilized phenol and benzene was examined by cloud point (CP), viscosity measurements, 1D and 2D NMR experiments, dynamic light scattering(DLS), and small angle neutron scattering (SANS) techniques.
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Tuning Nanoparticle-Micelle Interactions and Resultant Phase Behavior.
TL;DR: Results show that nanoparticle-surfactant micelle interactions can be tuned by the presence of electrolyte and/or choice of surfactant combination.
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Role of inter-micellar interaction on micellar growth
TL;DR: In this paper, small angle neutron-scattering and viscosity measurements from 0.1 M CTAC solutions with varying concentrations of KBr and KCl (C = 0.0-1.0 M) are reported.
23
Small-angle neutron scattering study of protein unfolding and refolding
TL;DR: The dilution method is used to show the refolding of unfolded proteins in the presence of urea and surfactant and the protein unfolding is shown to be reversible in all the above denaturating methods.