Time-delayed chameleon: Analysis,synchronization and FPGA implementation

In this paper we report a time-delayed chameleon-like chaotic system which can belong to different families of chaotic attractors depending on the choices of parameters. Such a characteristic of self-excited and hidden chaotic flows in a simple 3D system with time delay has not been reported earlier. Dynamic analysis of the proposed time-delayed systems are analysed in time-delay space and parameter space. A novel adaptive modified functional projective lag synchronization algorithm is derived for synchronizing identical time-delayed chameleon systems with uncertain parameters. The proposed time-delayed systems and the synchronization algorithm with controllers and parameter estimates are then implemented in FPGA using hardware–software co-simulation and the results are presented.     

Simple synthesis and spectroscopic studies on cobalt added ZnO nanocrystals

Cobalt doped zinc oxide nanoparticles were prepared through simple wet chemical method. X-ray diffraction studies confirm the prepared particles are in wurtzite structure. Scanning Electron Microscopy studies show the shape and morphology of the particles. To identify the presence of cobalt in ZnO, Energy Dispersive X-ray analysis was done. Optical absorption measurements show the presence of exciton peak at 375 nm. Photoluminescence studies were done with the excitation wavelength of 330 nm, which shows the emission because of exciton recombination and oxygen vacancy.     

Existence of solutions for impulsive neutral functional differential equations with nonlocal conditions

The existence, uniqueness and continuous dependence of a mild solution of an impulsive neutral functional differential evolution nonlocal Cauchy problem in general Banach spaces are studied, by using the fixed point technique and semigroup of operators.     

Proton-conducting I-Carrageenan-based biopolymer electrolyte for fuel cell application

The essential part of electrochemical devices, such as fuel cells and batteries, is the polymer electrolyte with good mechanical, thermal, and chemical stability. The search for a new proton-conducting membrane with easy processability, non-toxic, and low-cost has been growing rapidly. The bio-based polymer electrolytes are now receiving much attention due to the green environment. Among the commercially available biopolymers, iota-Carrageenan (I-Carrageenan) is one of the biopolymer with good film-forming nature and with good mechanical stability. I-Carrageenan-based biopolymer membranes doped with ammonium bromide (NH₄Br) have been prepared using solution-casting technique, and distilled water is used as a solvent. The prepared I-Carrageenan-based biopolymer membranes have been characterized using FTIR, XRD, and AC impedance techniques. The complexation between the polymer and salt has been revealed by FTIR. The increase in the amorphous nature of the film due to the addition of salt has been confirmed by XRD. From AC impedance technique, the conductivity of pure I-Carrageenan has been found to be 1.46 × 10⁻⁵ S/cm. The addition of different wt% of NH₄Br increases the conductivity and reaches the highest value of 1.08 × 10⁻³ S/cm for 20% NH₄Br, and the conductivity decreases on further addition of NH₄Br due to the formation of ion aggregates.

     

Lithium ion-conducting polymer electrolytes based on PVA–PAN doped with lithium triflate

Ionics - Blend polymer electrolytes with optimized composition (92.5 PVA:7.5 PAN) doped with lithium triflate (LiCF3SO3) have been prepared in different concentrations by solution casting...     

Carbon-supported Pd-Co as cathode catalyst for APEMFCs and validation by DFT

Carbon supported PdCo catalysts in varying atomic ratios of Pd to Co, namely 1 : 1, 2 : 1 and 3 : 1, were prepared. The oxygen reduction reaction (ORR) was studied on commercial carbon-supported Pd and carbon-supported PdCo nanocatalysts in aqueous 0.1 M KOH solution with and without methanol. The structure, dispersion, electrochemical characterization and surface area of PdCo/C were determined by X-ray diffraction (XRD), Transmission Electron Microscopy (TEM) and Cyclic Voltammetry (CV), respectively. The electrochemical activity for ORR was evaluated from Linear Sweep Voltammograms (LSV) obtained using a rotating ring disk electrode. The catalysts were evaluated for their electrocatalytic activity towards oxygen reduction reaction (ORR) in Alkaline Polymer Electrolyte Membrane Fuel Cells (APEMFCs). PdCo(3 : 1)/C gives higher performance (85 mW cm(-2)) than PdCo(1 : 1)/C, PdCo(2 : 1)/C and Pd/C. The maximum electrocatalytic activity for ORR in the presence of methanol was observed for PdCo(3 : 1)/C. First principles calculations within the framework of density functional theory were performed to understand the origin of its catalytic activity based on the energy of adsorption of an O(2) molecule on the cluster, structural variation and charge transfer mechanism.     

Origins of the stability of imidazole-imidazole, benzene-imidazole, and benzene-indole dimers: CCSD(T)/CBS and SAPT calculations

The respective structures and stabilities of imidazole-imidazole, benzene-imidazole, and benzene-indole dimers have been investigated using different DFT-D functional, MP2, CCSD(T), and SAPT levels of theory with a medium basis set. Comparative analysis of binding energies and structural parameters of the dimers points to a preference for stacking contact or hydrogen bond in an imidazole-imidazole dimer. In contrast, a T-shaped configuration with H-π interaction is maximally advantageous for benzene-imidazole and benzene-indole dimers. High-level ab initio calculations at the CCSD(T)/CBS and DFT-SAPT levels show that classical hydrogen-bonded tilted imidazole-imidazole dimer is a global minimum structure and that it has high electrostatic energy. However, for benzene-imidazole and benzene-indole dimers, the global minimum (N-H···π) structure has high electrostatic energy as well as dispersion energy.     

Helical peptide models for protein glycation: proximity effects in catalysis of the Amadori rearrangement.

INTRODUCTION: Non-enzymatic glycation of proteins has been implicated in various diabetic complications and age-related disorders. Proteins undergo glycation at the N-terminus or at the epsilon-amino group of lysine residues. The observation that only a fraction of all lysine residues undergo glycation indicates the role of the immediate chemical environment in the glycation reaction. Here we have constructed helical peptide models, which juxtapose lysine with potentially catalytic residues in order to probe their roles in the individual steps of the glycation reaction. RESULTS: The peptides investigated in this study are constrained to adopt helical conformations allowing residues in the i and i+4 positions to come into spatial proximity, while residues i and i+2 are far apart. The placing of aspartic acid and histidine residues at interacting positions with lysine modulates the steps involved in early peptide glycation (reversible Schiff base formation and its subsequent irreversible conversion to a ketoamine product, the Amadori rearrangement). Proximal positioning of aspartic acid or histidine with respect to the reactive lysine residue retards initial Schiff base formation. On the contrary, aspartic acid promotes catalysis of the Amadori rearrangement. Presence of the strongly basic residue arginine proximate to lysine favorably affects the pK(a) of both the lysine epsilon-amino group and the singly glycated lysine, aiding in the formation of doubly glycated species. The Amadori product also formed carboxymethyl lysine, an advanced glycation endproduct (AGE), in a time-dependent manner. CONCLUSIONS: Stereochemically defined peptide scaffolds are convenient tools for studying near neighbor effects on the reactivity of functional amino acid sidechains. The present study utilizes stereochemically defined peptide helices to effectively demonstrate that aspartic acid is an efficient catalytic residue in the Amadori arrangement. The results emphasize the structural determinants of Schiff base and Amadori product formation in the final accumulation of glycated peptides.