Optimization of ion energy spread in inductively coupled plasma source designed for focused ion beam applications

The ion energy distribution of inductively coupled plasma ion source for focused ion beam application is measured using a four grid retarding field energy analyzer. Without using any Faraday shield, ion energy spread is found to be 50 eV or more. Moreover, the ion energy distribution is found to have double peaks showing that the power coupling to the plasma is not purely inductive, but a strong parasitic capacitive coupling is also present. By optimizing the various source parameters and Faraday shield, ion energy distribution having a single peak, well separated from zero energy and with ion energy spread of 4 eV is achieved. A novel plasma chamber, with proper Faraday shield is designed to ignite the plasma at low RF powers which otherwise would require 300-400 W of RF power. Optimization of various parameters of the ion source to achieve ions with very low energy spread and the experimental results are presented in this article. (C) 2010 Elsevier Ltd. All rights reserved.

Microwave driven hydrothermal synthesis of LiMn2O4 nanoparticles as cathode material for Li-ion batteries

Among the various cathode materials studied for Li-ion batteries over the past many years, spinet LiMn2O4 is found to be one of the most attractive materials. Nanoparticles of the electrode materials sustain high rate capability due to large surface to volume ratio and small diffusion path length. Nanoparticles of spinel LiMn2O4 have been synthesized by microwave hydrothermal technique using prior synthesized amorphous MnO2 and LiOH. The phase and purity of spinel LiMn2O4 are confirmed by powder X-ray diffraction. The morphological studies have been investigated using field emission scanning electron microscopy and high-resolution transmission electron microscopy. The electrochemical performances of the material for Li insertion/extraction are evaluated by cyclic voltammetry, galvanostatic charge-discharge cycling and AC impedance studies. The initial discharge capacity is found to be about 89 mAh g(-1) at current density of 21 mA g(-1). (C) 2010 Elsevier B.V. All rights reserved.

Conformations of synthetic alamethicin fragments. Evidence for 310 helical folding from 270-MHz hydrogen-1 nuclear magnetic resonance and circular dichroism studies

IH NMR studies at 270 MHz on the synthetic alamethicin fragments Z-Aib-Pro-Aib-Ala-Aib-Ala-OMe (1-6), Boc-Gln-Aib-Val-Aib-Gly-Leu-Aib-OMe (7-1 3), Boc-Leu-Aib-Pro-Val-Aib-OMe (1 2-16), and Boc-Gly-Leu- Aib-Pro-Val-Aib-OMe (1 1-16) have been carried out in CDC13 and (CD3)2S0. The intramolecularly hydrogen bonded amide hydrogens in these peptides have been delineated by using solvent titration experiments and temperature coefficientsof NH chemical shifts in (CD3)+30. All the peptides adopt highly folded structures, characterized by intramolecular 4 - 1 hydrogen bonds. The 1-6 fragment adopts a 310 helical conformation with four hydrogen bonds, in agreement with earlier studies (Rao, Ch. P., Nagaraj, R., Rao, C. N. R., & Balaram, P. (1980) Biochemistry 19, 425-4311. The 7-13

An infrared spectroscopic study of C7 intramolecular hydrogen bonds in peptides

The ir-spectra in the N-H stretching region of Piv-Pro-NHMe and Boc-Pro-NHMe have been studied in carbon tetrachloride and chloroform solutions over a wide range of concentrations. Based on the concentration dependence of the N-H stretching bands, it has been shown that the characteristic N-H stretching band due to the C7 intramolecular hydrogen bond is around 3335 cm-'. Intermolecular hydrogen bonding also occurs to a small extent in these peptides, giving rise to a slight concentration dependence of the N-H stretching bands. The band around 3335 cm-* need not necessarily be due to C7 hydrogen bonds alone as proposed by Tsuboi et al. or to intermolecular hydrogen bonding alone as proposed by Maxfield et al.; this conclusion is supported by studies on Boc-Leu-NHMe, which undergoes only intermolecular hydrogen bonding We have shown that 2-Aib-Aib-OMe and Z-Aib- Ala-OMe form C7 intramolecular hydrogen bonds in addition to C5 intramolecular hydrogen bonds. The present studies also show that all the peptides studied exist in more than one conformation in solution.

A theory on the migration of an extraneous electron across hydrogen bonds in polypeptides

The migrating electrons in biological systems normally are extraneous and taking this into account the electron delocalisation across the hydrogen bonds in proteins is re-examined. It is seen that an extraneous electron can travel rapidly via the low-lying virtual orbitals of the hydrogen-bonded π-electronic structure of peptide units in proteins. The frequency of electron transfer decreases slowly with an increase in the path length. However, the coupling of electron and protonic motions enhances this frequency. Transfer of electrons across the hydrogen bonds in accordance with the double-exchange mechanism does not appear to be possible. This theory offers a possibility for an extraneous electron to transfer within protein structures.

N-H center dot center dot center dot F hydrogen bonds in fluorinated benzanilides: NMR and DFT study

Using F-19 and H-1-NMR (with N-14 decoupling) spectroscopic techniques together with density functional theoretical (DFT) calculations, we have investigated weak molecular interactions in isomeric fluorinated benzanilides. Simultaneous presence of through space nuclear spin-spin couplings ((1h)J(N-H center dot center dot center dot F)) of diverse strengths and feeble structural fluctuations are detected as a function of site specific substitution of fluorine atoms within the basic identical molecular framework. The transfer of hydrogen bonding interaction energies through space is established by perturbing their strengths and monitoring the effect on NMR parameters. Multiple quantum (MQ) excitation, up to the highest possible MQ orders of coupled protons, is utilized as a tool for accurate H-1 assignments. Results of NMR studies and DFT calculations are compared with the relevant structural parameters taken from single crystal X-ray diffraction studies.

Metallacarboranes: Toward Promising Hydrogen Storage Metal Organic Frameworks

Using first principles calculations, we show the high hydrogen storage capacity of metallacarboranes, where the transition metal (TM) atoms can bind up to 5 H-2-molecules. The average binding energy of similar to 0.3 eV/H favorably lies within the reversible adsorption range. Among the first row TM atoms, Sc and Ti are found to be the optimum in maximizing the H-2 storage (similar to 8 wt %) on the metallacarborane cluster. Being an integral part of the cage, TMs do not suffer from the aggregation problem, which has been the biggest hurdle for the success of TM-decorated graphitic materials for hydrogen storage. Furthermore, the presence of carbon atom in the cages permits linking the metallacarboranes to form metal organic frameworks, which are thus able to adsorb hydrogen via Kubas interaction, in addition to van der Waals physisorption.

Discharge studies in a triode ion plating system

A triode ion plating system with a hot cathode has been described. The performance of the system is studied, by studying the discharge behaviour from the bias voltage and bias current point of view, at the substrate, for different anode currents, filament voltages and pressures. The observed substrate bias current for different operating parameters is not found to be normal. The behaviour is explained on the bias of ionisation at the respective electrodes. The studies have revealed the importance of inter-electrode spacing in the enhancement of ionisation, in ion plating systems, at lower pressures.

C-H…O hydrogen bond mediated chain reversal in a peptide containing g-amino acid residue, determined directly from powder X-ray diffraction data

The finding that peptides containing -amino acid residues give rise to folding patterns hitherto unobserved in -amino acid peptides[1] has stimulated considerable interest in the conformational properties of peptides built from , and residues,[2] as the introduction of additional methylene (CH2) units into peptide chains provides further degrees of conformational freedom.

A C-H…O hydrogen bond stabilized polypeptide chain reversal motif at the C-terminus helices in proteins.

The serendipitous observation of a C–Hcdots, three dots, centeredO hydrogen bond mediated polypeptide chain reversal in synthetic peptide helices has led to a search for the occurrence of a similar motif in protein structures. From a dataset of 634 proteins, 1304 helices terminating in a Schellman motif have been examined. The C–Hcdots, three dots, centeredO interaction between the T−4 CαH and T+1 C=O group (Ccdots, three dots, centeredO≤3.5 Å) becomes possible only when the T+1 residue adopts an extended β conformation (T is defined as the helix terminating residue adopting an αL conformation). In all, 111 examples of this chain reversal motif have been identified and the compositional and conformational preferences at positions T−4, T, and T+1 determined. A marked preference for residues like Ser, Glu and Gln is observed at T−4 position with the motif being further stabilized by the formation of a side-chain–backbone Ocdots, three dots, centeredH–N hydrogen bond involving the side-chain of residue T−4 and the N–H group of residue T+3. In as many as 57 examples, the segment following the helix was extended with three to four successive residues in β conformation. In a majority of these cases, the succeeding β strand lies approximately antiparallel with the helix, suggesting that the backbone C–Hcdots, three dots, centeredO interactions may provide a means of registering helices and strands in an antiparallel orientation. Two examples were identified in which extended registry was detected with two sets of C–Hcdots, three dots, centeredO hydrogen bonds between (T−4) CαHcdots, three dots, centeredC=O (T+1) and (T−8) CαHcdots, three dots, centeredC=O (T+3).

Probing the role of the C-H center dot center dot center dot O hydrogen bond stabilized polypeptide chain reversal at the C-terminus of designed peptide helices. Structural characterization of three decapeptides

The structural characterization in crystals of three designed decapeptides containing a double D-segment at the C-terminus is described. The crystal structures of the peptides Boc-Leu-Aib-Val-Xxx-Leu-Aib-Val- (D)Ala-(D)Leu-Aib-OMe, (Xxx = Gly 2, (D)Ala 3, Aib 4) have been determined and compared with those reported earlier for peptide 1 (Xxx = Ala) and the all L analogue Boc-Leu-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe, which yielded a perfect right-handed a-helical structure. Peptides 1 and 2 reveal a right-handed helical segment spanning residues 1 to 7, ending in a Schellman motif with Ala(8) functioning as the terminating residue. Polypeptide chain reversal occurs at residue 9, a novel feature that appears to be the consequence of a C-(HO)-O-... hydrogen bond between residue 4 (CH)-H-alpha and residue 9 CO groups. The structures of peptides 3 and 4, which lack the pro R hydrogen at the C-alpha atom of residue 4, are dramatically different. Peptide 3 adopts a right-handed helical conformation over the 1 to 7 segment. Residues 8 and 9 adopt at conformations forming a C-terminus type I' beta-turn, corresponding to an incipient left-handed twist of the polypeptide chain. In peptide 4, helix termination occurs at Aib(6), with residues 6 to 9 forming a left-handed helix, resulting in a structure that accommodates direct fusion of two helical segments of opposite twist. Peptides 3 and 4 provide examples of chiral residues occurring in the less favored sense of helical twist; (D)Ala(4) in peptide 3 adopts an alpha(R) conformation, while (L)Val(7) in 4 adopts an alpha(L) conformation. The structural comparison of the decapeptides reported here provides evidence for the role of specific C-(HO)-O-... hydrogen bonds in stabilizing chain reversals at helix termini, which may be relevant in aligning contiguous helical and strand segments in polypeptide structures.