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Opposite Charges (opposite + charge)
Selected AbstractsChemically modified porous silicon for laser desorption/ionization mass spectrometry of ionic dyesJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 8 2009I. V. Shmigol Abstract Desorption/ionization on silicon (DIOS) mass spectra of model ionic dyes methylene blue (MB+Cl,) and methyl orange (Na+MO,) were studied using p+ type-derived porous silicon (PS) free layers. As-prepared PS (PS-H), the PS thermally oxidized at 300 °C (PS-OX), PS with chemically grafted cation-exchanging alkylsulfonic acid (PS-SO3H) and anion-exchanging propyl-octadecyldimethylammonium chloride (PS-ODMA+Cl,) groups was tested as ionization platforms. Two mechanisms of the methylene blue desorption/ionization were found: (1) the formation of [MB + H]+, ion due to the reduction/protonation of MB+, which is predominant for PS-H and PS-OX platforms and (2) direct thermal desorption of the MB+ cation, prevailing for PS-SO3H. The fragmentation of the cation is significantly suppressed in the latter case. The samples of PS-SO3H and PS-ODMA+ Cl, efficiently adsorb the dyes of the opposite charge from their solutions via the ion-exchange. Consequent DIOS MS studies allow to detect only low fragmented ions (MB+ and MO,, respectively), demonstrating the potential of the ion-exchange adsorption combined with DIOS MS for the analysis of ionic organic compounds in solutions. Copyright © 2009 John Wiley & Sons, Ltd. [source] Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysisPROTEIN SCIENCE, Issue 6 2008Dalei Wu Abstract Alanine racemase (Alr) is an important enzyme that catalyzes the interconversion of L-alanine and D-alanine, an essential building block in the peptidoglycan biosynthesis. For the small size of the Alr active site, its conserved substrate entryway has been proposed as a potential choice for drug design. In this work, we fully analyzed the crystal structures of the native, the D-cycloserine-bound, and four mutants (P219A, E221A, E221K, and E221P) of biosynthetic Alr from Escherichia coli (EcAlr) and studied the potential roles in substrate orientation for the key residues involved in the substrate entryway in conjunction with the enzymatic assays. Structurally, it was discovered that EcAlr is similar to the Pseudomonas aeruginosa catabolic Alr in both overall and active site geometries. Mutation of the conserved negatively charged residue aspartate 164 or glutamate 165 at the substrate entryway could obviously reduce the binding affinity of enzyme against the substrate and decrease the turnover numbers in both D- to L-Ala and L- to D-Ala directions, especially when mutated to lysine with the opposite charge. However, mutation of Pro219 or Glu221 had only negligible or a small influence on the enzymatic activity. Together with the enzymatic and structural investigation results, we thus proposed that the negatively charged residues Asp164 and Glu165 around the substrate entryway play an important role in substrate orientation with cooperation of the positively charged Arg280 and Arg300 on the opposite monomer. Our findings are expected to provide some useful structural information for inhibitor design targeting the substrate entryway of Alr. [source] Zeta Potential Measurement in Catalyst PreparationsCHEMICAL ENGINEERING & TECHNOLOGY (CET), Issue 2 2005J. B. Stelzer Abstract Oxide surfaces are covered with hydroxyl groups. In contact with water, positive or negative surface charges can be developed. The surface charge of oxide particles can be fine-tuned by changing the calcination temperature of the oxides before dispersion in water or by variation of the suspension pH. Strong negative or positive surface charges stabilize a suspension and avoid particle aggregation. Nano-structured catalysts suspended in water show surface charges different from those of compact TiO2. For spray drying, the cationic or anionic additives used have to be strongly attached via electrostatic forces to the surface of the suspended oxide particles. When noble metal complexes have to be brought to the support surface, the positively or negatively charged complexes must have an opposite charge relative to the surface charge. Zeta potential measurements can solve these problems. [source] Preparation and study of cellulose acetate membranes modified with linear polymers covalently bonded to Starburst polyamidoamine dendrimersJOURNAL OF APPLIED POLYMER SCIENCE, Issue 5 2008J. Ledesma-García Abstract Novel ion-selective membranes were prepared by means of the noncovalent modification of a cellulose acetate (CA) polymer with either poly(ethylene- alt -maleic anhydride) or poly(allylamine hydrochloride) chains covalently linked to Starburst amine-terminated polyamidoamine (PAMAM) dendrimers generations 4 and 3.5, respectively. Linear polymer incorporation within the porous CA membrane was performed with mechanical forces, which resulted in modified substrates susceptible to covalent adsorption of the relevant dendritic materials via the formation of amide bonds with a carbodiimide activation agent. The membranes thus prepared were characterized by chemical, physical, and spectroscopic measurements, and the results indicate that the dendrimer peripheral functional groups were the species that participated in the ion-exchange events. The prepared materials were also evaluated for their ion-exchange permeability with sampled current voltammetry experiments involving cationic and anionic species {[Ru(NH3)6]3+ and [Fe(CN6)]3,, respectively} as redox probe molecules under different pH conditions. As expected, although permeability was favored by opposite charges between the dendrimer and the electroactive probe, a clear blocking effect took place when the charge in the dendritic polymer and the electroactive complex was the same. Electrochemical impedance spectroscopy measurements, on the other hand, showed that the PAMAM-modified membranes were characterized by good selectivity and low resistance values for multivalent ions compared to a couple of commercial ion-exchange membranes. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2008 [source] Kinetics of the M-Intermediate in the Photocycle of Bacteriorhodopsin upon Chemical Modification with SurfactantsPHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 2 2010Li-Kang Chu The spectroscopic and kinetic studies of the interaction between bacteriorhodopsin in the M-intermediate and several surfactants (cetyl trimethyl ammonium bromide, dodecyl trimethyl ammonium bromide, diethylene glycol mono- n -hexyl ether, ethylene glycol mono- n -hexyl ether, sodium 1-decanesulfonate and sodium 1-heptanesulfonate) have been investigated using steady-state UV,VIS spectrometry and time-resolved absorption techniques. The steady-state spectral results show that bR retains its trimeric state. Time-resolved observations indicate that the rate of deprotonation of the protonated Schiff base increases in the presence of the cationic surfactants, whereas insignificant changes are observed in the neutral or anionic surfactants. The rate of the reprotonation of the Schiff base in the transition M , N is accelerated in anionic and neutral surfactants, but is decelerated in the presence of the cationic surfactants. Surfactants with a longer hydrocarbon tail have a greater effect on the kinetics when compared with surfactants having shorter hydrocarbon tails. The opposite effect is observed when the hydrophilic head of the surfactants contains opposite charges. These distinct kinetics are discussed in terms of the difference in the modified surface hydrophilicity of the bR and the possible protein configurational changes upon surfactant treatments. [source] Insulin adsorption into porous charged membranes: Effect of the electrostatic interactionBIOTECHNOLOGY PROGRESS, Issue 4 2009Shaoling Zhang Abstract Insulin adsorption into a series of porous charged membranes was investigated by batch adsorption experiments, and the experimental results were analyzed by the homogeneous diffusion model. The membranes used in this study were prepared by pore-surface modification of porous poly(acrylonitrile) (PAN) membranes by grafting with weak acidic and basic functional groups. The amount of insulin adsorbed into the membrane was determined from the material balance of insulin. The insulin partition coefficient K between the membrane and solution was estimated from the equilibrium adsorption amount, and the effective diffusion coefficient D was estimated by matching the model with the experimental data as a fitting parameter. The dependence of K and D on the charge properties of the insulin and membrane is observed and discussed. The partition coefficient K increased when the insulin and the membrane carried opposite charges, on the other hand, the effective diffusion coefficient D was reduced. These results indicate that the electrostatic interaction between the insulin and the membranes played an important role in the insulin adsorption. © 2009 American Institute of Chemical Engineers Biotechnol. Prog. 2009 [source] Modified Microperoxidases Exhibit Different Reactivity Towards Phenolic SubstratesCHEMBIOCHEM, Issue 12 2004Corrado Dallacosta Dr. Abstract The reactivity of several microperoxidase derivatives with different distal-site environments has been studied. The distal-site environments of these heme peptides include a positively charged one, an uncharged environment, two bulky and doubly or triply positively charged ones, and one containing aromatic apolar residues. The reactivity in the catalytic oxidation of two representative phenols, carrying opposite charges, by hydrogen peroxide has been investigated. This allows the determination of the binding constants and of the electron-transfer rate from the phenol to the catalyst in the substrate/microperoxidase complex. The electron-transfer rates scarcely depend on the redox and charge properties of the phenol, but depend strongly on the microperoxidase. Information on the disposition of the substrate in the adducts with the microperoxidases has been obtained through determination of the paramagnetic contribution to the1H NMR relaxation rates of the protons of the bound substrates. The data show that the electron-transfer rate drops when the substrate binds too far away from the iron and that the phenols bind to microperoxidases at similar distances to those observed with peroxidases. While the reaction rate of microperoxidases with peroxide is significantly smaller than that of the enzymes, the efficiency in the one-electron oxidation of phenolic substrates is almost comparable. Interestingly, the oxyferryl form of the triply positively charged microperoxidases shows a reactivity larger than that exhibited by horseradish peroxidase. [source] | |||||||||||||