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    Nanofiller-assisted Na+-conducting polymer nanocomposite for ultracapacitor: structural, dielectric and electrochemical properties
    (Springer, 2021-01-04T00:00:00) Kamboj, Vashu; Arya, Anil; Tanwar, Shweta; Kumar, Vijay; Sharma, A.L.
    We report the preparation of ZrO2 nanofiller-incorporated polymer nanocomposite electrolyte based on the PEO-NaPF6 matrix via standard solution cast method. The structure and morphology of polymeric films have been examined with X-ray diffraction and field emission scanning electron microscopy. Different interactions between the polymer, salt and nanofiller have been examined by Fourier transform infrared technique. The temperature-dependent (40�100��C) electrical conductivity has been examined from complex impedance spectroscopy (CIS). The highest ionic conductivity is exhibited by 5�wt% nanofiller-based electrolyte and recorded ~ 2 � 10�4�S�cm?1 at 100��C. The voltage stability window of polymeric film checked from linear sweep voltammetry is about ~ 4�V, and ion transference number close to unity confirms the major contribution from ion conduction. The dielectric properties have been explored in terms of complex permittivity, loss tangent and complex conductivity. The dielectric plots have been further fitted with an associated equation to evaluate principal dielectric parameters. The optimized polymer electrolyte possesses the lowest relaxation time and the highest dielectric constant that suggests the highest ionic conductivity, which is in good correlation with impedance results. The dc conductivity is also highest for the optimum system, and relaxation time decreases with an increase in temperature. The thermal stability of polymer electrolytes is about 200��C, as examined by thermogravimetric analysis (TGA). The ion transport parameters n, ?, D have been evaluated via FTIR, impedance spectroscopy and Bandara and Mellander (B�M) approach. Finally, the optimized polymer nanocomposite film has been used as an electrolyte-cum-separator for the fabrication of a solid-state symmetric supercapacitor. The electrochemical parameters specific capacitance, energy density, power density have been examined from cyclic voltammetry and galvanostatic charge�discharge technique. It may be concluded that nanofiller incorporation is an effective strategy to enhance the properties of electrolyte and has the potential to adopt as an electrolyte-cum-separator for ultracapacitor. � 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature.
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    Analysis of the effect of 1-Allyl-3-Methylimidazolium chloride on thermodynamic stability, folding kinetics, and motional dynamics of horse cytochrome c
    (Elsevier B.V., 2022-09-08T00:00:00) Garg, Mansi; Sharma, Deepak; Kumar, Rajesh
    1-allyl-3-methylimidazolium chloride (AMIMCl) acts as a potential green solvent for proteins. The present work provides a possible pathway by which the structural, kinetic, thermodynamic, and folding properties of horse cytochrome c (cyt c) are affected in green aqueous-AMIMCl systems. Analysis of the effect of AMIMCl on thermodynamic stability, refolding/unfolding kinetics, and motional dynamics of cyt c provided important information, (i) AMIMCl decreases the thermodynamic stability of reduced cyt c and also strengthens the guanidinium chloride (GdmCl)-mediated decrease in thermodynamic stability of protein, (ii) AMIMCl reduces the thermal-fluctuation of Met80-containing omega-loop of natively-folded compact state of carbonmonoxycytochrome c (MCO-state) due to polyfunctional interactions between the AMIM+ and different groups of protein, (iii) AMIMCl shifts the kinetic chevron plot, ln kobs[sbnd][GdmCl] to the lower concentration of GdmCl, (iv) AMIMCl shifts the refolding and unfolding limps to vertically downwards and upwards, respectively, and (v) AMIMCl reducing the unfolding free energy estimated by both thermodynamic and kinetic analysis. � 2022
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    Effect of imidazolium based ionic liquids on CO-association dynamics and thermodynamic stability of Ferrocytochrome c
    (Elsevier B.V., 2020-11-05T00:00:00) Garg, Mansi; Kumar, Sandeep; Kaur, Anupamjeet; Goyal, Bhupesh; Kumar, Rajesh
    Analysis of kinetic and thermodynamic parameters measured for CO-association reaction of Ferrocytochrome c (Ferrocyt c) under variable concentrations of 1-butyl-3-methylimidazolium with varying anion ([Bmim]X) (X = Cl?, I?, Br?, HSO4?) at pH 7 revealed that the low concentration of [Bmim]X (?0.5 M) constrains the CO-association dynamics of Ferrocyt c and typically follows the order: [Bmim]HSO4 > [Bmim]Cl > [Bmim]Br > [Bmim]I. At relatively higher concentrations (>0.5), the chaotropic action of [Bmim]+ dominates which consequently increases the thermal-fluctuations responsible to denature the protein and thus accelerates the speed of CO-association reaction. Analysis of thermal denaturation curves of Ferrocyt c measured at different concentrations of [Bmim]X revealed that the [Bmim]X decreases the thermodynamic stability of protein and typically follows the order: [Bmim]I > [Bmim]Br > [Bmim]Cl > [Bmim]CH3COO > [Bmim]HSO4, demonstrating that the effect of [Bmim]X on thermodynamic stability of protein is not in accordance to Hofmeister series effect of anions because instead of increasing the kosmotropic anion carrying [Bmim]X ([Bmim]CH3COO and [Bmim]HSO4) also decreases the thermodynamic stability of protein. � 2020 Elsevier B.V.
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    Factors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitro
    (Elsevier, 2018) Kumar, Rajesh; Sharma, Deepak; Kumar, Vinay; Kumar, Rajesh
    The role of crowding agents on structure and activities of heme proteins has been established. Analysis of kinetic and thermodynamic parameters measured for CO-dissociation reaction of natively-folded carbonmonoxycytochrome c (NCO) and carbonmonoxymyoglobin (MbCO) at different [GdnHCl] or [Urea] in the presence of crowding agents (dextran 40, dextran 70 and ficoll 70) demonstrate that (i) at low denaturant concentrations, crowder presence enhances the denaturant-mediated restricted dynamics of NCO and MbCO, and (ii) at higher denaturant concentrations, large scale unfolding-fluctuations dominate the dynamics and inclusion of crowder counteracts the structural-fluctuations causing the unfolding of proteins. Thermodynamic analysis of thermal and urea-unfolding curves of cytochrome c (Cyt c) and myoglobin (Mb) measured at different [GdnHCl] in presence of crowding agents reveals that crowder presence counterbalances and strengthens the destabilizing action of GdnHCl on stability of Cyt c and Mb, respectively. This study further demonstrates that the size, shape and concentration of crowding agent modulate the effect of crowder on denaturant-mediated dynamics and thermodynamic stability of heme proteins.