Indian Institute of Technology Indore

About: Indian Institute of Technology Indore is a education organization based out in Indore, Madhya Pradesh, India. It is known for research contribution in the topics: Fading & Support vector machine. The organization has 1606 authors who have published 4803 publications receiving 66500 citations.

Joint Impact of RF Hardware Impairments and Channel Estimation Errors in Spectrum Sharing Multiple-Relay Networks

Abstract: In this paper, we investigate the performance of a spectrum sharing decode-and-forward multiple-relay network (SSDMN) with direct link under the joint impact of two practical and detrimental imperfections, called transceiver hardware impairments (HIs) and channel estimation errors (CEEs). Here, we consider the hardware distortions induced by all the non-ideal secondary nodes and residual interferences originating from imperfect channel estimations. By taking these imperfections into account, we derive an exact closed-form expression for the outage probability of the considered SSDMN employing selection cooperation over independent and non-identical Rayleigh fading channels. We identify three important ceiling effects invoked by HIs, namely relay cooperation ceiling (RCC), direct link ceiling (DLC), and overall system ceiling. Specifically, we highlight the impact of these prevailing effects on the system’s performance and provide some useful insights about the tolerable level of HIs while designing the practical systems for a given rate requirement. We also illustrate that a potential direct link and a relaying link can, respectively, partially compensate for the incurred performance losses due to RCC and DLC effects. Moreover, we investigate the asymptotic behavior of outage probability to highlight the impact of HIs and CEEs on the achievable diversity and coding gains.

Interaction of different prototropic species of an anticancer drug ellipticine with HSA and IgG proteins: multispectroscopic and molecular modeling studies.

Abstract: Studies on interactions between an anticancer alkaloid, ellipticine, and various carrier proteins in blood serum show tangible results to gain insight into the solubility and transport of the drug under physiological conditions. In this report, we extensively studied the interactions of different prototropic species of ellipticine with two prominent serum proteins namely human serum albumin (HSA) and immunoglobulin G (IgG) in their native and partially unfolded states using steady state and time resolved fluorescence spectroscopy, molecular docking and circular dichroism (CD). Both the fluorescence techniques and molecular modeling studies elucidate that only neutral species of ellipticine binds to HSA in the sudlow site II. Unlike HSA, IgG in the native state mostly binds to cationic species of ellipticine. However, in partially unfolded configuration, IgG binds to the neutral ellipticine molecules. Molecular docking studies indicate the prevalence of electrostatic interactions involving charged residues in the binding process of cationic species of ellipticine with native IgG in its Fab region. In native conformation, the hydrophobic residues of the Fab region are found to be buried completely by the ligand. This implies that the hydrophobic interaction will be favored by unfolding of IgG through which the hydrophobic pocket will be more accessible to neutral species of ellipticine. The circular dichroism measurements reveal that upon interaction with ellipticine, heat and acid treated HSA resumes its α-helical content. This conclusive comparative study on interactions of IgG and HSA with ellipticine yields the result that native HSA is responsible for transport of neutral species of ellipticine whereas IgG carries cationic ellipticine in its native form.