Estimating specific yield and transmissivity with magnetic resonance sounding in an unconfined sandstone aquifer (Niger)

The unconfined aquifer of the Continental Terminal in Niger was investigated by magnetic resonance sounding (MRS) and by 14 pumping tests in order to improve calibration of MRS outputs at field scale. The reliability of the standard relationship used for estimating aquifer transmissivity by MRS was checked; it was found that the parametric factor can be estimated with an uncertainty a parts per thousand currency sign150% by a single point of calibration. The MRS water content (theta (MRS)) was shown to be positively correlated with the specific yield (Sy), and theta (MRS) always displayed higher values than Sy. A conceptual model was subsequently developed, based on estimated changes of the total porosity, Sy, and the specific retention Sr as a function of the median grain size. The resulting relationship between theta (MRS) and Sy showed a reasonably good fit with the experimental dataset, considering the inherent heterogeneity of the aquifer matrix (residual error is similar to 60%). Interpreted in terms of aquifer parameters, MRS data suggest a log-normal distribution of the permeability and a one-sided Gaussian distribution of Sy. These results demonstrate the efficiency of the MRS method for fast and low-cost prospection of hydraulic parameters for large unconfined aquifers.

Ab initio molecular dynamics simulations of excited hydrogen halides and methyl halides

Using excited-state ab initio molecular dynamics simulations employing the complete-active-space self-consistent-field approach, we study the mechanism of photodissociation in terms of time evolution of structure, kinetic energy, charges and potential energy for the first excited state of hydrogen halides and methyl halides. Although the hydrogen halides and methyl halides are similar in the photodissociation mechanism, their dynamics are slightly different. The presence of the methyl group causes delay in photodissociation as compared to hydrogen halides.

Trifurcated (four-center) hydrogen bond in solid state crystal structure of 5'-amino-5'-deoxyadenosine p-toluenesulfonate

The crystal structure of 5'-amino-5'-deoxyadenosine (5'-Am.dA) p-toluenesulfonate has been determined by X-ray crystallographic methods. It belongs to the orthorhombic space group P2(1)2(1)2(1) with a = 7.754(3)Angstrom, b = 8.065(1)Angstrom and c = 32.481(2)Angstrom. This nucleoside side shows a syn conformation about the glycosyl bond and C2'-endo-C3'-exo puckering for the ribose sugar. The orientation of N5' atom is gauche-trans about the exocyclic C4'-C5' bond. The amino nitrogen N5' forms a trifurcated hydrogen bond with N3, O9T and O4' atoms. Adenine bases form A.A.A triplets through hydrogen bonding between N6, N7 and N1 atoms of symmetry related nucleoside molecules.

Electrochemical reduction of hydrogen peroxide on stainless steel

Electrochemical reduction of hydrogen peroxide is studied on a sand-blasted stainless steel (SSS)electrode in an aqueous solution of NaClO4.The cyclic voltammetric reduction of H2O2 at low concentrations is characterized by a cathodic peak at -0 center dot 40 V versus standard calomel electrode(SCE).Cyclic voltammetry is studied by varying the concentration of H2O2 in the range from 0 center dot 2 mM to 20 mM and the sweep rate in the range from 2 to 100 mV s(-1)Voltammograms at concentrations of H2O2 higher than 2 mM or at high sweep rates consist of an additional current peak, which may be due to the reduction of adsorbed species formed during the reduction of H2O2. Amperometric determination of H2O2 at -0 center dot 50 V vs SCEprovides the detection limit of 5 A mu M H2O2. A plot of current density versus concentration has two segments suggesting a change in the mechanism of H2O2 reduction at concentrations of H2O2 a parts per thousand yen 2 mM. From the rotating disc electrode study, diffusion co-efficient of H2O2 and rate constant for reduction of H2O2 are evaluated.

Cu2+-induced room temperature hydrogen release from ammonia borane

Mechanical stirring of ammonia borane with CuCl2 in the solid state resulted in the release of hydrogen at room temperature through the intermediacy of [NH4](+)[BCl4](-).

Cytotoxicity of half sandwich ruthenium(II) complexes with strong hydrogen bond acceptor ligands and their mechanism of action

Neutral and cationic organometallic ruthenium(II) piano stool complexes of the type [(eta(6)-cymene)R-uCl(X)(Y)] (complexes R1-R8) has been synthesized and characterized. In cationic complexes, X, Y is either a eta(2) phosphorus ligand such as 1,1-bis(diphenylphosphino)methane (DPPM) and 1,2-bis(diphenylphosphino)ethane (DPPE) or partially oxidized ligands such as 1,2-bis(diphenylphosphino)methane monooxide (DPPMO) and 1,2-bis(diphenylphosphino)ethane monooxide (DPPEO) which are strong hydrogen bond acceptors. In neutral complexes. X is chloride and Y is a monodentate phosphorous donor. Complexes with DPPM and DPPMO ligands ([(eta(6)-cymene)Ru(eta(2)-DPPM)Cl]PF6 (R2), [(eta(6)-cymene)Ru(eta(2)-DPPMO)Cl]PF6 (R3), [(eta(6)-cymene)Ru(eta(1)-DPPM)Cl-2] (R5) and [(eta(6)-cymene)Ru(eta(1)-DPPMO)Cl-2] (R6) show good cytotoxicity. Growth inhibition study of several human cancer cell lines by these complexes has been carried out. Mechanistic studies for R5 and R6 show that inhibition of cancer cell growth involves both cell cycle arrest and apoptosis induction. Using an apoptosis PCR array, we identified the sets of antiapoptotic genes that were down regulated and pro-apoptotic genes that were up regulated. These complexes were also found to be potent metastasis inhibitors as they prevented cell invasion through matrigel. The complexes were shown to bind DNA in a non intercalative fashion and cause unwinding of plasmid DNA in cell-free medium by competitive ethidium bromide binding, viscosity measurements, thermal denaturation and gel mobility shift assays.

Aggregation of apolar peptides in organic solvents. Concentration dependence of 1H-nmr parameters for peptide NH groups in 310 helical decapeptide fragment of suzukacillin

Peptide NH chemical shifts and their temperature dependences have been monitored as a function of concentration for the decapeptide, Boc-Aib-Pro-Val-Aib-Val-Ala-Aib-Ala-Aib-Aib-OMe in CDCl3 (0.001-0.06M) and (CD3)2SO (0.001-0.03M). The chemical shifts and temperature coefficients for all nine NH groups show no significant concentration dependence in (CD3)2SO. Seven NH groups yield low values of temperature coefficients over the entire range, while one yields an intermediate value. In CDCl3, the Aib(1) NH group shows a large concentration dependence of both chemical shift and temperature coefficient, in contrast to the other eight NH groups. The data suggest that in (CD3)2SO, the peptide adopts a 310 helical conformation and is monomeric over the entire concentration range. In CDCl3, the 310 helical peptide associates at a concentration of 0.01M, with the Aib(1) NH involved in an intermolecular hydrogen bond. Association does not disrupt the intramolecular hydrogen-bonding pattern in the decapeptide.

Modulating the preferred O-H center dot center dot center dot O hydrogen-bonding motif in a conformationally constrained environment through hydroxy-group derivatization

The crystal structures of three conformationally locked esters, namely the centrosymmetric tetrabenzoate of all-axial per-hydronaphthalene- 2,3,4a, 6,7,8a-hexaol, viz. trans-4a, 8a-dihydroxyperhydronaphthalene-2,3,6,7-tetrayl tetrabenzoate, C38H34O10, and the diacetate and dibenzoate of all-axial perhydronaphthalene-2,3,4a, 8a-tetraol, viz. (2R*,3R*,4aS*,8aS*)-4a, 8a-dihydroxyperhydronaphthalene-2,3-diyl diacetate, C-14-H22O6, and (2R*, 3R*, 4aS*, 8aS*)-4a, 8a-dihydroxyperhydronaphthalene- 2,3-diyl dibenzoate, C24H26O6, have been analyzed in order to examine the preference of their supramolecular assemblies towards competing inter-and intramolecular O-H center dot center dot center dot O hydrogen bonds. It was anticipated that the supramolecular assembly of the esters under study would adopt two principal hydrogen-bonding modes, namely one that employs intermolecular O-H center dot center dot center dot O hydrogen bonds (mode 1) and another that sacrifices those for intramolecular O-H center dot center dot center dot O hydrogen bonds and settles for a crystal packing dictated by weak intermolecular interactions alone (mode 2). Thus, while the molecular assembly of the two crystalline diacyl derivatives conformed to a combination of hydrogen-bonding modes 1 and 2, the crystal packing in the tetrabenzoate preferred to follow mode 2 exclusively.

A direct borohydride fuel cell employing Prussian Blue as mediated electron-transfer hydrogen peroxide reduction catalyst

A direct borohydride-hydrogen peroxide fuel cell employing carbon-supported Prussian Blue (PB) as mediated electron-transfer cathode catalyst is reported. While operating at 30 °C, the direct borohydride-hydrogen peroxide fuel cell employing carbon-supported PB cathode catalyst shows superior performance with the maximum output power density of 68 mW cm−2 at an operating voltage of 1.1 V compared to direct borohydride-hydrogen peroxide fuel cell employing the conventional gold-based cathode with the maximum output power density of 47 mW cm−2 at an operating voltage of 0.7 V. X-ray diffraction (XRD), Scanning Electron Microscopy (SEM), and Energy Dispersive X-ray Analysis (EDAX) suggest that anchoring of Cetyl-Trimethyl Ammonium Bromide (CTAB) as a surfactant moiety on carbon-supported PB affects the catalyst morphology. Polarization studies on direct borohydride-hydrogen peroxide fuel cell with carbon-supported CTAB-anchored PB cathode exhibit better performance with the maximum output power density of 50 mW cm−2 at an operating voltage of 1 V than the direct borohydride-hydrogen peroxide fuel cell with carbon-supported Prussian Blue without CTAB with the maximum output power density of 29 mW cm−2 at an operating voltage of 1 V.

Expanding the Peptide beta-Turn in alpha gamma Hybrid Sequences: 12 Atom Hydrogen Bonded Helical and Hairpin Turns

Hybrid peptide segments containing contiguous alpha and gamma amino acid residues can form C-12 hydrogen bonded turns which may be considered as backbone expanded analogues of C-10 beta-turns) found in alpha alpha segments. Exploration of the regular hydrogen bonded conformations accessible for hybrid alpha gamma sequences is facilitated by the use of a stereochemically constrained gamma amino acid residue gabapentin (1-aminomethylcyclohexaneacetic acid, Gpn), in which the two torsion angles about C-gamma-C-beta (theta(1)) and C-beta-C-alpha (theta(2)) are predominantly restricted to gauche conformations. The crystal structures of the octapeptides Boc-Gpn-Aib-Gpn-Aib-Gpn-Aib-Gpn-Aib-OMe (1) and Boc-Leu-Phe-Val-Aib-Gpn-Leu-Phe-Val-OMe (2) reveal two distinct conformations for the Aib-Gpn segment. Peptide 1 forms a continuous helix over the Aib(2)-Aib(6) segment, while the peptide 2 forms beta-hairpin structure stabilized by four cross-strand hydrogen bonds with the Aib-Gpn segment forming a nonhelical C-12 turn. The robustness of the helix in peptide 1 in solution is demonstrated by NMR methods. Peptide 2 is conformationally fragile in solution with evidence of beta-hairpin conformations being obtained in methanol. Theoretical calculations permit delineation of the various C-12 hydrogen bonded structures which are energetically feasible in alpha gamma and gamma alpha sequences.

Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin

he crystal structure of 12 peptides containing the conformationally constrained 1-(aminomethyl)cyclohexaneacetic acid, gabapentin (Gpn), are reported. In all the 39 Gpn residues conformationally characterized so far, the torsion angles about the C-alpha-C-beta and C-beta-C-gamma bonds are restricted to the gauche conformation (+/- 60 degrees). The Gpn residue is constrained to adopt folded conformations resulting in the formation of intramolecularly hydrogen-bonded structures even in short peptides. The peptides Boc-Ac(6)c-Gpn-OMe 1 and Boc-Gpn-Aib-Gpn-Aib-OMe 2 provide examples of C-7 conformation; peptides Boc-Gpn-Aib-OH 3, Boc-Ac(6)c-Gpn-OH 4, Boc-Val-Pro-Gpn-OH 5, Piv-Pro-Gpn-Val-OMe 6, and Boc-Gpn-Gpn-Leu-OMe 7 provide examples of C-9 conformation; peptide Boc-Ala-Aib-Gpn-Aib-Ala-OMe 8 provides an example of C-12 conformation and peptides Boc-beta Leu-Gpn-Val-OMe 9 and Boc-beta Phe-Gpn-Phe-OMe 10 provide examples of C-13 conformation. Gpn peptides provide examples of backbone expanded mimetics for canonical alpha-peptide turns like the gamma (C-7) and the beta (C-10) turns. The hybrid beta gamma sequences provide an example of a mimetic of the C-13 alpha-turn formed by three contiguous alpha-amino acid residues. Two examples of folded tripeptide structures, Boc-Gpn-beta Phe-Leu-OMe 11 and Boc-Aib-Gpn-beta Phg-NHMe 12, lacking internal hydrogen bonds are also presented. An analysis of available Gpn residue conformations provides the basis for future design of folded hybrid peptides.

Hydrophobic Peptide Channels and Encapsulated Water Wires

Peptide nanotubes with filled and empty pores and close-packed structures are formed in closely related pentapeptides. Enantiomorphic sequences, Boc-(D)Pro-Aib-Xxx-Aib-Val-OMe (Xxx = Leu, 1; Val, 2; Ala, 3; Phe, 4) and Boc-Pro-Aib-(D)Xxx-Aib-(D)Val-OMe ((XXX)-X-D = (D)Leu, 5; (D)Val, 6; (D)Ala, 7; (D)Phe, 8), yield molecular structures with a very similar backbone conformation but varied packing patterns in crystals. Peptides 1, 2, 5, and 6 show tubular structures with the molecules self-assembling along the crystallographic six-fold axis (c-axis) and revealing a honeycomb arrangement laterally (ab plane). Two forms of entrapped water wires have been characterized in 2: 2a with d(O center dot center dot center dot O) = 2.6 angstrom and 2b with d(O center dot center dot center dot O) = 3.5 angstrom. The latter is observed in 6 (6a) also. A polymorphic form of 6 (6b), grown from a solution of methanol-water, was observed to crystallize in a monoclinic system as a close-packed structure. Single-file water wire arrangements encapsulated inside hydrophobic channels formed by peptide nanotubes could be established by modeling the published structures in the cases of a cyclic peptide and a dipeptide. In all the entrapped water wires, each water molecule is involved in a hydrogen bond with a previous and succeeding water molecule. The O-H group of the water not involved in any hydrogen bond does not seem to be involved in an energetically significant interaction with the nanotube interior, a general feature of the one-dimensional water wires encapsulated in hydrophobic environements. Water wires in hydrophobic channels are contrasted with the single-file arrangements in amphipathic channels formed by aquaporins.

An alkaline direct borohydride fuel cell with hydrogen peroxide as oxidant

A novel alkaline direct borohydride fuel cell (ADBFC) using varying concentrations of hydrogen peroxide as oxidant and sodium borohydride with sodium hydroxide, each of differing concentration, as fuel is reported. A peak power density of ca. 150 in W cm(-2) at a cell voltage of 540 mV can be achieved from the optimized ADBFC operating at 70 degrees C. (c) 2004 Elsevier B.V. All rights reserved.

Vector Evaluated Particle Swarm Optimization (VEPSO) of Supersonic Ejector for Hydrogen Fuel Cells

Fuel cells are emerging as alternate green power producers for both large power production and for use in automobiles. Hydrogen is seen as the best option as a fuel; however, hydrogen fuel cells require recirculation of unspent hydrogen. A supersonic ejector is an apt device for recirculation in the operating regimes of a hydrogen fuel cell. Optimal ejectors have to be designed to achieve best performances. The use of the vector evaluated particle swarm optimization technique to optimize supersonic ejectors with a focus on its application for hydrogen recirculation in fuel cells is presented here. Two parameters, compression ratio and efficiency, have been identified as the objective functions to be optimized. Their relation to operating and design parameters of ejector is obtained by control volume based analysis using a constant area mixing approximation. The independent parameters considered are the area ratio and the exit Mach number of the nozzle. The optimization is carried out at a particularentrainment ratio and results in a set of nondominated solutions, the Pareto front. A set of such curves can be used for choosing the optimal design parameters of the ejector.

Peptide mimics for structural features in proteins. Crystal structures of three heptapeptide helices with a C-terminal 6-->1 hydrogen bond.

The crystal structure determination of three heptapeptides containing alpha-aminoisobutyryl (Aib) residues as a means of helix stabilization provides a high-resolution characterization of 6-->1 hydrogen-bonded conformations, reminiscent of helix-terminating structural features in proteins. The crystal parameters for the three peptides, Boc-Val-Aib-X-Aib-Ala-Aib-Y-OMe, where X and Y are Phe, Leu (I), Leu, Phe (II) and Leu, Leu (III) are: (I) space group P1, Z = 1, a = 9.903 A, b = 10.709 A, c = 11.969 A, alpha = 102.94 degrees, beta = 103.41 degrees, gamma = 92.72 degrees, R = 4.55%; (II) space group P21, Z = 2, a = 10.052 A, b = 17.653 A, c = 13.510 A, beta = 108.45 degrees, R = 4.49%; (III) space group P1, Z = 2 (two independent molecules IIIa and IIIb in the asymmetric unit), a = 10.833 A, b = 13.850 A, c = 16.928 A, alpha = 99.77 degrees, beta = 105.90 degrees, gamma = 90.64 degrees, R = 8.54%. In all cases the helices form 3(10)/alpha-helical (or 3(10)helical) structures, with helical columns formed by head-to-tail hydrogen bonding. The helices assemble in an all-parallel motif in crystals I and III and in an antiparallel motif in II. In the four crystallographically characterized molecules, I, II, IIIa and IIIb, Aib(6) adopts a left-handed helical (hL) conformation with positive phi, psi values, resulting in 6-->1 hydrogen-bond formation between Aib(2) CO and Leu(7)/Phe(7) NH groups. In addition a 4-->1 hydrogen bond is seen between Aib(3) CO and Aib(6) NH groups. This pattern of hydrogen bonding is often observed at the C-terminus of helices proteins, with the terminal pi-type turn being formed by four residues adopting the hRhRhRhL conformation.