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Random Dirac fermions and localisation phenomena in one dimensionSteiner, Margit Susanne January 1999 (has links)
No description available.
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Weighted two-particle Green's functions in the coherent-potential approximation and perturbation effects in tunneling systems out of equilibriumSchwabe, Nikolai F. January 1996 (has links)
No description available.
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Redox Reactions at Oil-Water Interface by Particle Collision ElectroanalysisPaul, Dilip K 01 January 2018 (has links)
Particle Collision Electrochemistry (PCE) has gained considerable attention in heterogeneous catalysis, petroleum chemistry and pharmaceutical fields. The PCE refers to a phenomenon in which a particle strikes on an inert electrode surface as a consequence of its Brownian motion and produces a spike of current for the direct oxidation/reduction of the individual particle. This method allows us characterization of individual particles and in-situ study of electrochemical reactions coupled to the particle.
Herein, emulsion droplets were studied by PCE where toluene droplets contained hydrophobic tetrachloro-1,4-benzoquinone (Q). This was investigated as a model system to study the molecular effects that arise due to hydrogen bonding reagents (oleic acid, acetic acid) inside and outside of the droplets. The emulsions were prepared by sonicating toluene-quinone solution with the water phase containing an ionic liquid to provide conductivity to the droplet. Each droplet produced a current spike while colliding with the electrode surface that was held at a potential to reduce tetrachoro-1,4-benzoquinone. In bulk acetonitrile and toluene, tetrachoro-1,4-benzoquinone undergoes a two electron reduction process to form the tetrachloro phenolate di-anion (Q2-). It was shown that the hydrogen bonding affinity of Q2- for acetic acid (pKa = 4.8) was higher than for oleic acid (pKa = 9.9) for both bulk systems (as acetic acid is stronger hydrogen bonding donor than oleic acid). However, the reversed trend was observed in emulsified toluene droplets when studied by PCE. This was attributed to the preferential partition of the carboxylic acids between the two phases in the emulsion. Oleic acid stays inside the droplets due its hydrophobic nature and hydrogen bonding with Q2- takes place inside the droplet. In contrast, solvation of acetic acid by the surrounding water, causes the hydrogen bonding with Q2- to occur significantly less inside the droplet.
Another redox system studied by PCE was hydrophobic ferrocene (Fc) trapped in the toluene droplet to determine the effect of surfactant on the particle size. The diameter determined electrochemically was compared with Dynamic Light Scattering (DSL) measurements. The presence of nonionic surfactant (triton X-100) was observed to affect the droplet’s size easily monitored by PCE. The mediated oxidation of cysteine by the oxidized Fc inside the droplet was investigated at different concentrations of cysteine.
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Structural studies of the bacteriophage lambda holin and M. tuberculosis secA translocaseSavva, George Christos 15 May 2009 (has links)
Double stranded DNA bacteriophages achieve release of phage progeny by disrupting the cell envelope of the host cell. This is accomplished by two phage-encoded proteins, the holin and the endolysin. In bacteriophage lambda, the S holin is a small three TMD membrane protein that creates a lesion in the inner membrane of the host at a specific time, programmed in its primary structure. Lesion formation permits the cytoplasmic endolysin R access to the murein cell wall for degradation and cell lysis. Although it has been shown that S oligomerizes in the membrane, the structural nature of this complex has not been elucidated. In this study the S holin was purified using a mild non-ionic detergent and the structure of a ring complex formed by the holin was determined by electron microscopy and single particle analysis at a resolution of 2.6 nm. Biochemical characterization of the rings suggests that such a complex might represent the assembly formed by S in the membrane. Protein translocation in all organisms allows the export of proteins destined for localization outside the cytoplasm. In eubacteria, newly synthesized proteins are directed to the heterotrimeric membrane complex SecYEG by signals embedded in their sequence. The driving force through this complex is provided by the cytoplasmic ATPase SecA which combines ATP hydrolysis to mechanically insert proteins through the protein conducting channel. Using electron microscopy and single particle analysis we have obtained the structure of SecA from M. tuberculosis. The structure indicates that four SecA monomers assemble to form an elongated molecule with D2 symmetry. Docking of the EM map to the crystal structure of tb SecA confirms this arrangement of the subunits. This finding, that M. tuberculosis SecA forms a tetramer raises intriguing possibilities about SecA function.
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Structural studies of the bacteriophage lambda holin and M. tuberculosis secA translocaseSavva, George Christos 15 May 2009 (has links)
Double stranded DNA bacteriophages achieve release of phage progeny by disrupting the cell envelope of the host cell. This is accomplished by two phage-encoded proteins, the holin and the endolysin. In bacteriophage lambda, the S holin is a small three TMD membrane protein that creates a lesion in the inner membrane of the host at a specific time, programmed in its primary structure. Lesion formation permits the cytoplasmic endolysin R access to the murein cell wall for degradation and cell lysis. Although it has been shown that S oligomerizes in the membrane, the structural nature of this complex has not been elucidated. In this study the S holin was purified using a mild non-ionic detergent and the structure of a ring complex formed by the holin was determined by electron microscopy and single particle analysis at a resolution of 2.6 nm. Biochemical characterization of the rings suggests that such a complex might represent the assembly formed by S in the membrane. Protein translocation in all organisms allows the export of proteins destined for localization outside the cytoplasm. In eubacteria, newly synthesized proteins are directed to the heterotrimeric membrane complex SecYEG by signals embedded in their sequence. The driving force through this complex is provided by the cytoplasmic ATPase SecA which combines ATP hydrolysis to mechanically insert proteins through the protein conducting channel. Using electron microscopy and single particle analysis we have obtained the structure of SecA from M. tuberculosis. The structure indicates that four SecA monomers assemble to form an elongated molecule with D2 symmetry. Docking of the EM map to the crystal structure of tb SecA confirms this arrangement of the subunits. This finding, that M. tuberculosis SecA forms a tetramer raises intriguing possibilities about SecA function.
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Detecting single-particle insulating collisions in microfluidics as a function of flow rateNettleton, Elizabeth Grace 27 February 2013 (has links)
This work presents the first electrochemical observation of single polystyrene microbead collisions with an electrode within a microchannel. We have observed that detecting single microbead collisions is facile with this system. Additionally, we have shown that by increasing flow within the channel, one can increase both the frequency and magnitude of collision signals. This technique may provide a means of signal amplification in future sensing work. / text
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Investigating high-j single-particle energies in Z = 51 nucleiMitchell, Alan John January 2012 (has links)
The work of this thesis consists of a systematic study of low-lying, proton single-particle states in Z = 51 isotopes. States in 113−125Sb were populated via (α,t) and (3He,d) single-proton adding reactions, performed on stable even tin isotopes. The Yale tandem accelerator delivered beams of 37.5-MeV α particles and 25-MeV 3He nuclei for the reactions. Outgoing tritons and deuterons were momentum analysed using an Enge split-pole spectrometer. To obtain absolute cross sections, the product of target thickness and spectrometer aperture size was calibrated for each target, using sub-Coulomb α- particle elastic scattering. States were observed up to ∼4 MeV excitation energy. Angular momentum transfer assignments were made through comparison of angular distributions and ratios of cross sections between different reactions. Relative spectroscopic factors ex- tracted through a DWBA analysis allowed energy centroids of the observed single-particle strength to be reconstructed.These measurements build upon the results of a previous (α,t) study, which was per- formed on the same targets. The previous measurements estimated that ∼ 90% of the πg7/2 and πh11/2 strength was held in the lowest-lying 7/2+ and 11/2− states, respectively. The difference in energy of these states increased with increasing neutron excess, and al- though they were in agreement with theoretical calculations that included contributions of the tensor interaction, poor statistics limited the information obtained regarding the weak fragments of high-j single-particle strength. Careful examination of these fragments, with the use of greater statistics, has been performed in this work. The (3He,d) measurements aid in making l transfer assignments and provide complementary information regarding the low-j states.Binding energies of the πg7/2 and πh11/2 orbitals measured in this work were compared to the energies of the lowest-lying 7/2+ and 11/2− states and theoretical calculations that include the tensor interaction. Though shifted higher in energy due to the fragmentation, trends in the centroids appear to be consistent with the lowest-lying states. The trend of the πg7/2–πh11/2 energy difference is in quantitative agreement with the predicted effects of the tensor interaction, with increasing neutron excess.
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Structural Analysis of Arabidopsis thaliana CDC48A ATPase using Single Particle Cryo-Electron MicroscopyAldakheel, Lila A. 05 1900 (has links)
Cdc48A and its human homologue P97 are from ATPase family, which play a variety of roles in cellular activates and it has a crucial involvement in protein quality control pathways. It is best known for its involvement in endoplasmic reticulum associated protein degradation (ERAD), where it mediates the degradation of the aggerated or misfolded proteins by the proteasome. Considering the multiple functions of Cdc48A in many protein regulatory processes, it is a potential therapeutic target for neurogenerative diseases and cancer. Cdc48A polypeptide comprises N domain, followed by D1 and D2 domains respectively that are joined by linkers, whereas functionally it forms a homo hexameric complex. Since Cdc48A is from the ATPase family, it uses the ATP hydrolysis to generate a mechanical force with its co-factors to perform its functions. There are many cofactors that interact with Cdc48A and two of them are Ufd1-NpI4 which in turn interact with ubiquitinated proteins from the ER membrane. The mechanism linking the conversion of the energy of ATP hydrolysis into mechanical force and unfolding the substrate is vague. My aim is to reconstruct a first 3D- model of plant Cdc48A using single particle cryo-EM, which serves the basis to conduct more detailed mechanistic studies towards substrate unfolding and threading/unfolding in the future. In general, results showed one defined structure of cdc48A at ~ 9.8 Å, which is the ADP-ATP conformation. Although another other structure was also resolved at ~ 8.9 Å, it was hard to characterize due to its dissimilarity with known structures of Cdc48A homologues and thus requires further characterization.
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Détection et caractérisation des nanoparticules de dioxyde de titane dans les aliments par AF4-ICP-MS et Sp-ICP-MS / Detection and characterization of titanium dioxide nanoparticles by AF4-ICP-MS and Sp-ICP-MSGivelet, Lucas 21 June 2019 (has links)
Les travaux de thèse portent sur le développement de méthodes pour la caractérisation des nanoparticules (NPs) de dioxyde de titane (TiO2) dans les aliments. L’étude a été séparée distinctement en deux axes. Le développement de la méthode AF4-ICP-MS (I) au sein de la Plateforme Nano-Sécurité du CEA de Grenoble et le développement de la méthode Sp-ICP-MS (II) au sein du Laboratoire de la Sécurité Aliments de l’Anses à Maisons-Alfort.Pour le premier axe, les interactions électrostatiques entre les particules et la membrane de l’AF4 ont été étudiées. La charge de surface (potentiel zêta) a été mesuré pour différentes type de particule et membrane en fonction de plusieurs paramètres du solvant tel que le pH, la force ionique ainsi que la présence de tensio-actifs. Suite aux nombreuses analyses effectuées plusieurs conditions de solvant ont été identifiées comme favorable à la répulsion électrostatique entre les particules et la membrane ce qui permettrai de diminuer les pertes de particules au niveau de la membrane. Plusieurs conditions ont donc été testées directement pour l’analyse de NPs de TiO2 en AF4-ICP-MS. Il a ainsi été montré que les conditions favorisant les répulsions électrostatiques permettaient d’améliorer le taux dé récupération des particules au niveau du système AF4. Cependant les analyses ont aussi montré que les NPs de TiO2 n’étaient pas suffisamment dispersées pour pouvoir obtenir une distribution en taille fiable.Le second volet de la thèse, a eu pour but, dans un premier temps, d’optimiser le traitement de données de la méthode Sp-ICP-MS. Plusieurs améliorations ont été réalisées comme le calcul automatique du seuil bruit de fond-particule, le calcul de l'efficacité de transport où encore l'ajout de paramètres de contrôle qualité. Ce traitement de données a ensuite été comparée à un logiciel dédié aux analyses par Sp-ICP-MS et a permis de mettre en avant que la feuille de calcul interne donne des résultats avec une meilleure justesse, tout en fournissant des paramètres supplémentaires.Dans un second temps une optimisation de la méthode Sp-ICP-MS a été réalisée. Plusieurs paramètres ont donc été évalués comme le choix de l’isotope de titane, le temps d’acquisition, le type de solvant pour disperser les particules, ainsi que le mode de prélèvement de l’échantillon et son débit.Enfin, plusieurs aliments ont été analysés après avoir mis en place un protocole d’extraction des NPs. Les résultats obtenus ont permis de déterminer une distribution en taille des NPs de TiO2 présentes dans les échantillons. / The thesis focuses on the development of methods for the titanium dioxide (TiO2) nanoparticles (NPs) characterization in food products. The study was separated distinctly into two axes. The development of the AF4-ICP-MS (I) method within the CEA Nano-Safety Platform in Grenoble and the development of the Sp-ICP-MS (II) method within the Food Safety Laboratory of the Anses in Maisons-Alfort.For the first axis, the electrostatic interactions between the particles and the AF4 membrane were studied. The surface charge (zeta potential) was measured for particles and membranes depending on several solvent parameters such as pH, ionic strength and the presence of surfactants. Following the several analyzes carried out, several solvent conditions have been identified as promoting the electrostatic repulsion between the particles and the membrane, which will make it possible to reduce the losses of particles at the level of the membrane. Several conditions were therefore directly tested for NPs analysis of TiO2 in AF4-ICP-MS. It has thus been shown that the conditions favoring electrostatic repulsions make it possible to improve the efficiency of the particles at the level of the AF4 system. However, the analyzes also showed that the TiO2 NPs were not sufficiently dispersed to obtain a reliable size distribution.The second part of the thesis aimed at first optimizing the data treatment of the Sp-ICP-MS method. Several improvements have been made such as the automatic calculation of the background-particle threshold, the calculation of the transport efficiency or the addition of quality control parameters. This data treatment was then compared to a software dedicated to analyzes by Sp-ICP-MS and made it possible to highlight that the internal spreadsheet gives results with a better accuracy, while providing additional parameters.In a second time an optimization of the Sp-ICP-MS method was carried out. Several parameters were therefore evaluated such as the choice of the titanium isotope, the acquisition time, the type of solvent to disperse the particles, as well as the sample collection mode and its flow rate.Finally, several foods were analyzed after setting up an extraction protocol for NPs. The results obtained made it possible to determine a size distribution of the NPs of TiO2 present in the samples.
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Structural biology of Cystic Fibrosis Transmembrane Conductance Regulator, an ATP-binding cassette protein of medical importanceAlzahrani, Ateeq Ahmed Hassan January 2012 (has links)
The cystic fibrosis transmembrane conductance regulator (CFTR) is a transmembrane protein that functions as an ion channel. Mutations in this protein cause Cystic Fibrosis. For this reason, it is important to study the structure and function of CFTR. In this study, constructs of CFTR (C-terminii), a CFTR-interacting protein and full-length CFTR were cloned, expressed and purified for structural and functional studies. The purified C-terminal polypeptides of CFTR were soluble and shown to interact with NHERF1 PDZ 1 (a CFTR-interacting protein). The CFTR C-terminus and NHERF1 PDZ 1 domain were co-expressed and co-purified. The purified complex showed a strong interaction that might induces a conformational change. Site-directed mutation of the C-terminus of CFTR was performed in order to examine the effect of removing a potentially flexible amino acid (Arginine) on protein crystallization. Pull-down assay experiments with full-length CFTR demonstrated an interaction between CFTR (in DDM detergent) and NHERF1 PDZ 1(+). No interaction was observed for CFTR in LPG (a relatively denaturing detergent) and NHERF1, implying that the interaction between the PDZ motive of CFTR and NHERF1 requires a stable folded structure for both proteins. In addition, full-length CFTR in DDM has been studied by electron microscopy and Single Particle Analysis in the presence of NHERF1 PDZ 1(+). A 3D structure was generated for the CFTR-NHERF1 PDZ 1(+) complex at a resolution of ~ 18 A. This 3D structure showed a new open conformation of CFTR (V shape). In comparable studies with CFTR alone, a 3D structure was generated at a resolution of 27 A and this structure showed a closed state as previously reported. This new data suggest a possible role for NHERF1 in terms of CFTR channel gating or activation.
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