Articles written in Journal of Chemical Sciences
Volume 119 Issue 5 September 2007 pp 343-350
Recent optical kerr effect (OKE) studies have revealed that orientational relaxation of rodlike nematogens near the isotropic-nematic (I-N) phase boundary and also in the nematic phase exhibit temporal power law decay at intermediate times. Such behaviour has drawn an intriguing analogy with supercooled liquids. Here, we have investigated the single-particle and collective orientational dynamics of a family of model system of thermotropic liquid crystals using extensive computer simulations. Several remarkable features of glassy dynamics are on display including non-exponential relaxation, dynamical heterogeneity, and non-Arrhenius temperature dependence of the orientational relaxation time. Over a temperature range near the I-N phase boundary, the system behaves like a fragile glass-forming liquid. Using proper scaling, we construct the usual relaxation time versus inverse temperature plot and explicitly demonstrate that one can successfully define a density dependent fragility of liquid crystals. The fragility of liquid crystals shows a temperature and density dependence which is remarkably similar to the fragility of glass forming supercooled liquids. Energy landscape analysis of inherent structures shows that the breakdown of the Arrhenius temperature dependence of relaxation rate occurs at a temperature that marks the onset of the growth of the depth of the potential energy minima explored by the system.
Volume 124 Issue 1 January 2012 pp 317-325
Dielectric dispersion and NMRD experiments have revealed that a significant fraction of water molecules in the hydration shell of various proteins do not exhibit any slowing down of dynamics. This is usually attributed to the presence of the hydrophobic residues (HBR) on the surface, although HBRs alone cannot account for the large amplitude of the fast component. Solvation dynamics experiments and also computer simulation studies, on the other hand, repeatedly observed the presence of a non-negligible slow component. Here we show, by considering three well-known proteins (
Volume 129 Issue 7 July 2017 pp 841-847 REGULAR ARTICLE
Size and structure of cytochrome c (Cyt C) bound to gold nano-clusters (AuNC) were studied using fluorescence correlation spectroscopy (FCS) and circular dichroism (CD) spectroscopy. The CD spectra of Cyt C indicate that the ellipticity is almost completely lost on binding to AuNC which indicates unfolding.Addition of ethanol causes partial restoration of ellipticity and hence, structure of Cyt C. FCS data indicate that size (hydrodynamic radius, rH) of free Cyt C is 17Å which increases to 24Å on binding to AuNC. This too suggests unfolding of Cyt C upon binding to AuNCs. Both the size and conformational relaxation time of Cyt C bound to AuNC vary non-monotonically with increase in ethanol content.
Volume 132, 2019
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