Дисертації з теми "Sulfur Peptide"
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Hippauf, Felix. "Tailoring Pore Size and Polarity for Liquid Phase Adsorption by Porous Carbons." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-223482.
Повний текст джерелаChappell, Paul Elliott. "Structural studies of peptide binding to chicken class I MHC molecules, the CD6-CD166 interaction and enzymes involved in bacterial sulfur metabolism." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:d4fa5a1b-530b-4a10-8184-02742cfa34f6.
Повний текст джерелаYamamoto, Masaru. "Synthesis and oxidation studies of sulfur containing inhibitors for human leukocyte elastase : (2) synthesis of cyclic peptide analogs for tissue factor pathway inhibitor (TFPI) : Part 2 synthesis and evaluation of aziridinecarboxylic acid analogs as a new family of cysteine proteinase inhibitors." Diss., Georgia Institute of Technology, 1993. http://hdl.handle.net/1853/25953.
Повний текст джерелаValer, Luca. "Histidine ligated Iron-Sulfur Proteins and Peptides." Doctoral thesis, Università degli studi di Trento, 2022. https://hdl.handle.net/11572/355641.
Повний текст джерелаMatteucci, Mizio. "Solid phase synthesis and applications of sulfur bridged peptides." Thesis, University of Southampton, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.274652.
Повний текст джерелаHautier, Alexandre. "Synthesis and characterization of copper-peptide systems for oxidation catalysis." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0758.
Повний текст джерелаCatalysis gives access to efficient transformations at a lower cost in energy and generally offers possibilities to reduce or eliminate the need for and the generation of hazardous compounds . The development of a catalyst is often inspired by Nature that performs challenging chemical transformations with high rates and high selectivity under mild conditions and aqueous media. For example, copper dependent proteins can react to oxidize a broad range of substrates. Inspired by biological systems, metallopeptides have recently emerged as reliable platforms to evolve new catalysts because they are chemically accessible, easy to handle and fine-tune.In this work we synthetized a family of bioinspired decapeptides containing His and Asp residues as metal ion coordinating amino acids. Their copper coordination properties were studied using pH potentiometry, and different spectroscopic techniques (UV-Vis, CD, EPR, NMR). The data indicates that all the peptides bind copper and form similar major copper(II) species at a pH close to neutrality where copper (II) is coordinated by the side-chains of His and Asp residues. Finally, the capabilities of these metallopeptides to perform a variety of oxidative transformations in aqueous solution at room temperature, using H2O2 as the oxidant were evaluated in parallel with that of amyloid-β peptides copper (II) complexes. This study revealed that i) the scaffold of the designed peptides had an impact on the catalytic efficiencies and enantiomeric excess and ii) the amyloid-β peptides copper (II) complexes are less active than our designed copper(II) peptide systems
Srour, Batoul. "Emerging roles for natural and artificial lipids in shaping the catalytic function, stability and oligomeric state of membrane proteins." Thesis, Strasbourg, 2015. http://www.theses.fr/2015STRAF068/document.
Повний текст джерелаThe study of biological membranes involves the examination of the different properties of its main components: as lipids and proteins. In this manuscript, the lipid-lipid interaction and the lipid-protein interaction were monitored by vibrational spectroscopy (Raman and Infrared). We have been interested in the first part in studying the structure and organization of phospholipids in the gel phase and the liquid crystalline phase using mid infrared spectroscopy. In addition, the effect of the head group composition on the hydrogen bonding behaviour of lipid mixtures was probed using far infrared spectroscopy. In the second part, the interaction of the NADH ubiquinone oxidoreductase protein and NuoL mutant (D563N) with zinc was investigated through FTIR difference spectroscopy where the conformational changes upon zinc binding were monitored. Finally, the metal-ligand vibrations of the iron- sulfur clusters in NuoB mutants (C64A G100C) at different pH were analysed using Raman spectroscopy
Rossetto, Daniele. "Emergence, survival, and selection of metal-binding peptides in the prebiotic environment." Doctoral thesis, Università degli studi di Trento, 2022. https://hdl.handle.net/11572/355344.
Повний текст джерелаImani, Zeynab. "Le rôle d’interactions N-H···S proximales dans des peptides." Thesis, université Paris-Saclay, 2021. http://www.theses.fr/2021UPASF015.
Повний текст джерелаNon-covalent interactions play a key role in chemical biology phenomena such as the stabilization of protein tertiary and quaternary structure or protein-protein and protein-substrate recognition. Among these interactions, the classical amide-type NH···O=C hydrogen bond has been thoroughly studied. The study of other types of non-covalent interactions implicating peptide backbone NH groups is much rarer. This work focused on the impact of NH···S hydrogen bonding on the conformational preferences of thioether amino acid residues and their short oligomers. A panel of capped derivatives of the following non-canonical sulfur-containing amino acids was prepared: Cys(Me) (acyclic), Attc (thietane), Atlc (thiolane), Atc (thiane). These derivatives were characterized computationally, by IR/UV double resonance laser spectroscopy in the gas phase, by IR and NMR spectroscopy in solution, and in the solid state. We demonstrated the concomitant existence of inter-residue C6ˠ NH···S hydrogen bonds and C5 NH···O=C interactions in each of these four compounds. This combined stabilizing feature was also prevalent in Attc oligomers. A different intra-residue C5ˠ NH···S hydrogen bond was characterized in short oligomers of Atlc and Atc, in some cases associated with a ˠ-turn NH···O=C interaction. The significance of NH···S bonding in the combined C5-C6ˠ structural feature of Attc was evaluated by comparison with capped derivatives of other four-membered ring amino acids: Ac4c (cyclobutane), Aatc(Me) (azetidine), Aotc (oxetane). The C5–C6ˠ feature was present in the three heterocyclic residues: comparison of their IR spectra in gas phase and in solution, aided by theoretical calculations, allowed us to identify an increasing strength of NH···X hydrogen bonding from X=O to X=S to X=N
Hadjidakis, I. "Studies relating to the ferrodoxins : The influence of synthetic peptides on the assembly of iron-sulphur clusters." Thesis, University of Exeter, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.353046.
Повний текст джерелаVon, Borowski Rafael Gomes. "Avaliação da atividade antibiofilme de Capsicum baccatum var. pendulum (Solanaceae)." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2015. http://hdl.handle.net/10183/149467.
Повний текст джерелаMany species of Capsicum red peppers are used in traditional medicinal practices. These plants are utilized in a number of preparations to treat a variety of illnesses including infections. Some bacteria produce biofilm as an important virulence factor, due to this its structure mediates the adhesion to surfaces as implanted devices, probes, catheters and also promotes physical protection against the antibiotics or the immune system response. Accordingly, this study investigated the ability of the extract and isolated products from seeds of Capsicum baccatum as anti-biofilm agent. This study demonstrates by the first time that an extract from C. baccatum presented relevant anti-biofilm activity against Staphylococcus epidermidis and Pseudomonas aeruginosa. The active fraction was obtained by bio-guided assays and analyzed by HPLC-DAD-MS, MALDI-TOF MS and MALDI-MS/MS, identifying it as peptides from 2S sulfur-rich seed storage protein 2-like. It strongly controlled (2mg/ml) the S. epidermidis biofilm formation (>96%) when the compound was in solution and adsorbed on Permanox™ slides. Interestingly, it did not inhibit the growth of this bacterium, indicating the inhibition of biofilm is independent of bacterial cell death. Moreover, this peptides preserved human erythrocytes and lymphocytes integrity after 24-48 h of exposure, suggesting the fractionation potentiated the anti-biofilm activity of the C. baccatum crude extract while absolutely reduced its cytotoxicity. Our results corroborate to the search of new non-antibiotic strategies to combat microorganisms with a reduced pressure for resistance development.
Vo, Chau Duy Tam. "Etude biochimique de trois nouvelles protéines impliquées dans la biosynthèse de l’ubiquinone en anaérobie chez Escherichia coli : UbiT, UbiU et UbiV A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone Ubiquinone Biosynthesis over the Entire O 2 Range: Characterization of a Conserved O 2-Independent Pathway." Thesis, Sorbonne université, 2019. https://accesdistant.sorbonne-universite.fr/login?url=http://theses-intra.upmc.fr/modules/resources/download/theses/2019SORUS401.pdf.
Повний текст джерелаUbiquinone (UQ) is a polyprenylated lipid that plays an important role in electron transport in the respiratory chains of E. coli. The aerobic biosynthesis of UQ in E. coli requires eight reactions and involves at least twelve proteins (UbiA-UbiK and UbiX). In this work, we demonstrate that seven Ubi proteins form the Ubi complex, a stable metabolon that catalyzes the last six reactions of the UQ biosynthetic pathway. The X-Ray structure of the SCP2 domain of UbiJ forms an extended hydrophobic cavity that could bind UQ intermediates inside the 1-MDa Ubi complex. The Ubi complex is purified from cytoplasmic extracts and UQ biosynthesis occurs in this fraction, challenging the current thinking of a membrane-associated biosynthetic process. UQ is reported to be biosynthesized under both anerobic and anaerobic conditions. We characterize a novel, O2-independent pathway for the biosynthesis of UQ. This pathway relies on three proteins, UbiT, UbiU, and UbiV. UbiT contains an SCP2 lipid-binding domain and is likely an accessory factor of the biosynthetic pathway, while UbiU and UbiV (UbiU-UbiV) are involved in hydroxylation reactions and represent a novel class of O2-independent hydroxylases. We demonstrate that UbiU-UbiV from E.coli form a heterodimer, wherein each protein binds a [4Fe-4S] cluster via conserved cysteines that are essential for activity. Moreover, we show that purified UbiU from P. aeruginosa is able to bind UQ, suggesting a different role of UbiU and UbiV. UbiU and UbiV belong to peptidase U32 family whose function remains questionable. By bioinformatic analyses, we demonstrated that U32 proteins were characterized by four conserved cysteines important for their enzymatic activities and by biochemical tools, we confirmed that RlhA and TrhP, two others U32 subfamilies, like UbiU and UbiV, are all Fe-S proteins
Giada, Maria de Lourdes Reis. "Isolamento, caracterização e quantificação de peptídeos y-glutamil sulfurados no feijão (Phaseolus vulgaris L.)." Universidade de São Paulo, 1995. http://www.teses.usp.br/teses/disponiveis/9/9131/tde-22082017-092501/.
Повний текст джерелаThe non-protein fraction of Phaseolus vulgrias L. seeds has been analysed to obtain information on the identity and level of (γ-glutamyl peptides containing a sulfur amino acid. These peptides (γ-glutamyl-S-methylcysteine and (γ-glutamyl methionine) could interfere with the determination of methionine measured by cleavage with cyanogen bromide and subsequent gas-chromatographic identification of methylthiocyanate. The ethanolic extract of (γ-glutamyl peptides contains 21% of the total seed nitrogen, which decrease to 5,5%, by removing the coextracted bean proteins with chloroform. This non-protein extract was then purified by ion-exchange chromatography on basic and acid resins, taking advantage of the different pK values of the amino acids. The isolation procedure was followed up by chemical analysis, thin layer chromatography and amino acid analysis. Based on their chemical properties we were able to identify the presence of S-methylcysteine, mainly in the form of a dipeptide with glutamic acid. Quantitative analysis of the peptide after acid hydrolysis (3h /110° C) showed a level of 0,67g /total S-methylcysteine /100gbean protein. This content accounted for approximately 50% of the bean methionine content, determined by ion-exchange chromatography. These results might indicate that total methylthiocyanate released from both, methionine and S-methylcysteine of beans, (1,6%) (from a previous paper) subtracted from S-methylcysteine (0,7%) could be recognized as chemically available methionine, corresponding to approximately 64% of total methionine. During seed germination the (γ-glutamyl-S-methylcysteine undergo a degradative process resulting in loss of the dipeptide.
Schreiner, Eduard [Verfasser]. "Biochemical aspects of iron-sulfur systems : magnetostructural properties of ferredoxins and prebiotic peptide synthesis involving pyrite / Eduard Schreiner." 2007. http://d-nb.info/986316598/34.
Повний текст джерелаHippauf, Felix. "Tailoring Pore Size and Polarity for Liquid Phase Adsorption by Porous Carbons." Doctoral thesis, 2016. https://tud.qucosa.de/id/qucosa%3A30276.
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