Dissertations / Theses on the topic 'Proteins thiol'
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Le, Min. "Protein coimmobilization: Reactions of vicinal thiol groups of proteins /." The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487946776021788.
Full textKantner, Terrence. "Bioconjugation strategies through thiol-alkylation of peptides and proteins." Thesis, University of Bath, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.675737.
Full textPennisi, Manuela. "Redox proteomics, thiol homeostasis and neurophysiologicla correlations in aging and neurodegeneration." Doctoral thesis, Università di Catania, 2014. http://hdl.handle.net/10761/1533.
Full textGough, Jonathan David Lees Watson J. "Aromatic thiol based redox buffers increasing the folding rates of disulfide containing proteins /." Related electronic resource: Current Research at SU : database of SU dissertations, recent titles available full text, 2004. http://wwwlib.umi.com/cr/syr/main.
Full textHall, Michael. "The chloroplast lumen : New insights into thiol redox regulation and functions of lumenal proteins." Doctoral thesis, Umeå universitet, Kemiska institutionen, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-58423.
Full textLui, James Kwok Ching. "A fluorescent labelling technique to detect changes in the thiol redox state of proteins following mild oxidative stress." University of Western Australia. School of Biomedical, Biomolecular and Chemical Sciences, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0056.
Full textZhang, Yun. "Mass Spectrometric Analysis of Thiol Proteins/Peptides Following Selenamide Derivatization And Electrolytic Reduction of Disulfide Bonds." Ohio University / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1347395762.
Full textHameed, Rana Majeed. "The application of aqueous two phase systems to the analysis of protein isoforms of importance in clinical biochemistry and biopharmaceutical production." Thesis, Brunel University, 2016. http://bura.brunel.ac.uk/handle/2438/14452.
Full textSafazadeh, Haghighi Leila. "DESIGN OF HIGHLY STABLE LOW-DENSITY SELF-ASSEMBLED MONOLAYERS USING THIOL-YNE CLICK REACTION FOR THE STUDY OF PROTEIN-SURFACE INTERACTIONS." UKnowledge, 2016. http://uknowledge.uky.edu/cme_etds/61.
Full textKade, Ige Joseph. "Interaction of organodiselenides with sulphydryl groups at the active sites of some thiol containing proteins - in vitro and in vivo mechanistic studies in mammalian models of diabetes." Universidade Federal de Santa Maria, 2008. http://repositorio.ufsm.br/handle/1/4398.
Full textO presente estudo quis comparar os potenciais antioxidants in vitro de organoselênios novamente sintetizados, diseleneto dicolesterol e diseleneto de difenila e suas possíveis interações com algumas enzimas contendo tióis em diferentes tecidos de mamíferos. Além disso, o potencial de DPDS como agente antioxidante e antihiperglicêmico, e sua interação com proteínas contendo tióis em vários tecidos e órgãos de mamíferos (hepático, renal, esplênico e, mais importante, tecido cerebral) foram avaliados em modelos animais de streptozotocina induzindo diabetes em ratos. Os resultados in vitro mostram que DPDS exibiu uma maior atividade mimética da glutationa peroxidase bem como aumentada habilidade para oxidar mono e di-tióis que DPDS. Além disso, enquanto o DPDS inibiu substâncias reativas ao ácido tiobarbitpúrico (TBARS) e formação de proteínas carboniladas em tecidos cerebral e hepático, induzidas por ferro(II) ou SNP, DCDS exibiu um efeito pró-oxidante em cérebro e tecido hepático quando ferro(II) serviu como próoxidante, porém, quando TBARS foi induzido por SNP, DCDS modificou a formação de TBARS tanto em tecido cerebral como hepático. Também, as atividades da deltaaminolevulinato desidratase (ð-ALA-D) cerebral e hepática e Na+/K+-ATPase cerebral foram significativamente inibidas por DPDS e somente fracamente inibida por DCDS. Mas estudos revelam que a inibição causada por organodiselenetos (neste caso, DPDS) na atividade da Na+/K+-ATPase envolve a modificação de grupos tiólicos ligados ao sítio ATP da enzima. Similarmente, diferentes isoformas da lactato desidrogenase (LDH) foram significativamente inibidas por DPDS e DCDS in vitro. nós observamos que a inibição in vitro de diferentes isoformas da LDH por DCDS e DPDS envolve a modificação de grupos SH no sítio ligante NAD+ da enzima. a administração oral de DPDS dissolvido em óleo soya administrado a ratos albino machos com diabetes induzida por streptozotocina mostrou que houve uma redução significante nos níveis de glicose sanguínea acompanhada por uma marcada redução nas proteínas glicadas em ratos diabéticos induzidos com streptozitocina tratados com DPDS em relação aos não diabéticos. Além disso, DPDS melhorou significativamente os níveis de vitamina C e GSH (fígado, rim e baço), que foram diminuídos em ratos tratados com streptozotocina. Similarmente, tratamento com DPDS marcadamente aboliu os níveis elevados de TBARS que foram observados no grupo diabético. Finalmente, a inibição da ð-ALA-D e algumas isoformas da LDH causada pela hiperglicemia foram prevenidas por DPDS. Nós também observamos que STZ provocou uma significante diminuição no status antioxidante do cérebro e atividade da Na+/K+- ATPase, mas a atividade da acetilcolinesterase e captação e liberação de glutamato não foram alteradas. Porém, DPDS marcadamente restaurou o desequilíbrio observado no status antioxidante e bomba de sódio. Finalmente, nós concluímos que organoselenetos são remédios antioxidantes promissores no manejo de doenças causadas por estresse oxidativo. Porém, sua toxicidade envolve uma interação com tióis em proteínas e este estudo demonstrou que os grupos sulfidril em questão são críticos para a função normal de enzimas e proteínas. Estes SH são associados com tióis dos sítios de ligação do substrato (sítio ativo) de enzimas. interessantemente, doses farmacológicas de organodiselenetos (3mg/kg para o estudo de diabetes) não apresentou nenhuma toxicidade observada.
Appolinario, Patricia Postilione. "Avaliação do efeito do ácido docosahexaenoico e de seus hidroperóxidos na oligomerização de SOD1 em um modelo da doença esclerose lateral amiotrófica." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-06082013-082744/.
Full textALS is a progressive and fatal disease caused by selective degeneration of motor neurons in the brain and spinal cord. Twenty percent of familial ALS (fALS) cases are caused mainly by point mutations in the sod1 gene. Docosahexaenoic acid (C22:6, n-3, DHA) is a highly unsaturated fatty acid, wich is one of the main fatty acids in the cerebral gray matter. Studies have linked SOD1 mutations to the formation of aggregates that could be induced by unsaturated fatty acids. The aim of this study was to evaluate the effect of DHA on aggregation of SOD1 fALS mutants in vitro and its mechanisms. CD analysis shows changes in the secondary structure of both apo-SOD1WT and G93A promoted by DHA resulting in an increase in the surface hydrophobicity and formation of structures such as beta amyloid, which was also confirmed by bis-ANS assay and Thioflavin, respectively. These changes enhance the interaction of SOD1 and DHA, leading to amorphous aggregates as revealed by FESEM. Incubation of DHA with apo-SOD1 forms results in high-molecular weight species as detected by SDS-PAGE analyses under non-reducing conditions and also by size exclusion chromatography. This appears to require Cys residues in their thiolate forms because high aggregates are not observed under reducing conditions and also by size exclusion chromatography or at acidic pH. Also, size-exclusion chromatography indicates that the mutant apo-SOD1 aggregation is dependent on the unsaturation and cis-conformation of fatty acids. Compared to the DHA, DHAOOH had a minor effect on SOD1 aggregation, however revealed the ability to induce covalent dimerization of SOD1. Overall, the data suggest a mechanism of DHA aggregation, by a process involving exposure to hydrophobic surfaces, formation of disulfide bonds and also for possible cross-links involving reactions such \"thiol-ene\".
ASTORI, EMANUELA. "IN VITRO AND IN VIVO APPROACHES TO STUDY OXIDATIVE STRESS, ANEMIA AND DYSBIOSIS IN CHRONIC KIDNEY DISEASE." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/818976.
Full textCosta, N. J. "Mitochondrial protein thiol modifications during oxidative stress." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598052.
Full textCarvalho, Larissa Anastácio da Costa. "Efeito pró-oxidante do hidroperóxido de urato sobre proteínas sensíveis às alterações redox: implicações na resposta inflamatória." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-22082017-104057/.
Full textUrate hydroperoxide (HOOU) is the product of the oxidation of uric acid by peroxidases. The formation of HOOU is favored during inflammation and in hyperuricemia, where there is plenty amount of uric acid, inflammatory peroxidases and superoxide. Therefore, the aim of the present study was to evaluate the effect of urate hydroperoxide on redox sensitive proteins in an inflammatory environment and another that mimics infection. In this thesis the chemical structure of the HOOU produced by photo-oxidation was compared to that obtained by myeloperoxidase catalysis. The chemical production of HOOU allowed a better purification of the compound. This oxidant was able to specifically react with sulfur containing amino acids (methionine and cysteine). In this sense, its reactivity with peroxiredoxins (Prx1 and Prx2) was investigated. HOOU reacted fast with Prx1 k = 4.9 × 105 M-1s-1 and Prx2 k = 2.3 × 106 M-1s-1. In addition, HOOU was able to oxidize Prx2 from intact erythrocytes at the same extend as does hydrogen peroxide. Albumin is an important thiol-containing protein to redox homeostasis in plasma. HOOU was able to oxidize albumin with a rate constant of 0.2 × 102 M-1s-1. Another protein with important function in redox homeostasis is thioredoxin (Trx). Trx was oxidized by HOOU with a rate constant of 2.8 × 102 M-1s-1 and was released together with Prx1 and Prx2 from human macrophages cells (THP-1 cell line) that were incubated with HOOU. The release of these proteins is a signal of cellular stress. Thus, HOOU may be involved in the exacerbation of oxidative stress in inflammatory environments. When neutrophil (HL-60 cell line) and macrophages (THP-1 cell line) were incubated with uric acid and Pseudomonas aeruginosa there was a decrease in hypochlorous acid (HOCl) production because of the competition between chloride and uric acid by myeloperoxidase. It decreased HOCl and impaired the microbicidal activity of the cells, showing that HOOU does not contribute in bacteria clearance. Therefore, the oxidation of uric acid to urate hydroperoxide impairs microbicidal activity and oxidizes thiol-proteins in inflammatory cells contributing to a pro-oxidant status. In this context, the antioxidant role of uric acid in inflammatory response should be reviwed.
Patel, Amar S. "Synthesis of Aromatic Monothiols and Aromatic Dithiols to Increase the Folding Rate and Yield of Disulfide Containing Proteins." FIU Digital Commons, 2010. http://digitalcommons.fiu.edu/etd/313.
Full textPrincipe, P. D. L. "Quantitative studies of cellular protein thiol groups in relation to the growth behaviour of rat liver cell lines : Comparative estimations by computerised microdensitometry, biochemistry and flow cytometry." Thesis, Brunel University, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382988.
Full textMatsusaki, Motonori. "Molecular Mechanism of Oxidative Protein Folding by Soybean Protein Thiol Disulfide Oxidoreductases/ERO1 Pathway." Doctoral thesis, Kyoto University, 2016. http://hdl.handle.net/2433/217183.
Full text0048
新制・課程博士
博士(農学)
甲第20008号
農博第2192号
新制||農||1045(附属図書館)
学位論文||H28||N5017(農学部図書室)
33104
京都大学大学院農学研究科農学専攻
(主査)教授 裏出 令子, 教授 松村 康生, 教授 三上 文三
学位規則第4条第1項該当
Doctor of Agricultural Science
Kyoto University
DFAM
Matsusaki, Motonori. "Molecular Mechanism of Oxidative Protein Folding by Soybean Protein Thiol Disulfide Oxidoreductases / ERO1 Pathway." Kyoto University, 2009. http://hdl.handle.net/2433/217183.
Full text0048
新制・課程博士
博士(農学)
甲第20008号
農博第2192号
新制||農||1045(附属図書館)
学位論文||H28||N5017(農学部図書室)
33104
京都大学大学院農学研究科農学専攻
(主査)教授 裏出 令子, 教授 松村 康生, 教授 三上 文三
学位規則第4条第1項該当
Hotchkiss, Kylie A. Medical Sciences Faculty of Medicine UNSW. "Regulation of Thrombospondin 1 Structure / Function by Intramolecular Thiol-Disulfide Isomerization." Awarded by:University of New South Wales. Medical Sciences, 2009. http://handle.unsw.edu.au/1959.4/44770.
Full textTong, Grace C. "Characterization of Cys-34 in serum albumin." Columbus, Ohio : Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc%5fnum=osu1061473878.
Full textTitle from first page of PDF file. Document formatted into pages; contains xxiii, 325 p.; also contains graphics (some col.). Includes abstract and vita. Advisor: Gary E. Means, Dept. of Biochemistry. Includes bibliographical references (p. 206-225).
Cannon, Mark Brimhall. "Re-engineering redox-sensitive green flourescent protein as indicators of cellular thiol oxidation status /." view abstract or download file of text, 2005. http://wwwlib.umi.com/cr/uoregon/fullcit?p3181089.
Full textTypescript. Includes vita and abstract. Includes bibliographical references (leaves 75-82). Also available for download via the World Wide Web; free to University of Oregon users.
Hurd, T. R. "Interactions between mitochondrial protein thiols and reactive oxygen species." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604824.
Full textThiel, Philipp [Verfasser], and Oliver [Akademischer Betreuer] Kohlbacher. "Computational Methods for the Modulation of Protein-Protein Interactions / Philipp Thiel ; Betreuer: Oliver Kohlbacher." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1163320862/34.
Full textDegefa, Tesfaye Hailu. ""Ion channel (mimetic) sensors" mechanism of charge propagation through thiol-, protein- and dendrimer-modified electrodes /." Doctoral thesis, [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=980218624.
Full textWang, Zhengfang. "Thiol Protein/Peptide Modification by N-(Phenylseleno)phthalimide and Applications of Chemometrics in Organic Food Authentication." Ohio University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1395159533.
Full textGroß, Christine [Verfasser], Kay [Akademischer Betreuer] Hamacher, and Gerhard [Akademischer Betreuer] Thiel. "In Silico Studies on Proteins for Synthetic Biology / Christine Groß ; Kay Hamacher, Gerhard Thiel." Darmstadt : Universitäts- und Landesbibliothek Darmstadt, 2019. http://d-nb.info/1176701967/34.
Full textJunior, Carlos Abrunhosa Tairum. "Investigação de transições estruturais e da reatividade sobre peróxidos de Tsa1p (Thiol Specific Antioxidant Protein 1) de Saccharomyces cerevisiae." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/87/87131/tde-03122015-200158/.
Full text2-Cys Prx constitute a group of homodimeric antioxidant enzymes that act in the decomposition of hydroperoxides using a reactive cysteine (peroxidase cysteine - CysP). The high reactivity of the CysP is achieved by the participation of two vicinal amino acids: a threonine and an arginine, which constitute the catalytic triad. After the decomposition of hydroperoxide, the CysP forms an intermolecular disulfide with a second cysteine residue (resolving cysteine - CysR), which is reduced by the thioredoxin (Trx). During the redox cycle, these enzymes undergo to changes in the structure, but the molecular mechanisms involved in this process were poorly understood. In this study we have obtained the crystallographic structure of the 2-Cys Prx enzyme Tsa1 from Saccharomyces cerevisiae. By means of biochemical and molecular biology approaches, the importance of amino acids involved in reactivity and structural transitions were determined. Finally, efforts have been performed to the determination of the crystallographic structures of mutant proteins obtained in this study.
Greiner, Timo [Verfasser], Gerhard [Akademischer Betreuer] Thiel, and Adam [Akademischer Betreuer] Bertl. "Characterization of novel potassium transport proteins from Chlorella viruses / Timo Greiner. Betreuer: Gerhard Thiel ; Adam Bertl." Darmstadt : Universitäts- und Landesbibliothek Darmstadt, 2011. http://d-nb.info/1105563049/34.
Full textPichelin-Poitevin, Dominique. "Marquage differentiel de proteines membranaires par des inhibiteurs de thiols en presence de saccharose et de divers analogues." Poitiers, 1987. http://www.theses.fr/1987POIT2260.
Full textPaterson, Andrea Beth. "Mechanisms of acetaminophen-induced hepatotoxicity, effects of mitochondrial glutathione, protein thiols and oxidative phosphorylation." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/mq22375.pdf.
Full textKoç, Cengiz [Verfasser], and Thilo [Akademischer Betreuer] Stehle. "Structures and functions of proteins that utilize and modify Wall Teichoic Acid / Cengiz Koç ; Betreuer: Thilo Stehle." Tübingen : Universitätsbibliothek Tübingen, 2016. http://d-nb.info/1165309386/34.
Full textDietrich, Melanie [Verfasser], and Thilo [Akademischer Betreuer] Stehle. "Neutralization Recognition and Structural Features of Reovirus Attachment Protein σ1 / Melanie Dietrich ; Betreuer: Thilo Stehle." Tübingen : Universitätsbibliothek Tübingen, 2019. http://d-nb.info/1176509357/34.
Full textPeixoto, Álbert Souza. "Oxidação da proteína dissulfeto isomerase por peroxinitrito: cinética, produtos e implicações biológicas." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-14122017-142837/.
Full textProtein disulfide isomerase (PDI) is a ubiquitous dithiol-disulfide oxidoreductase that performs an array of cellular functions, including in cellular signaling and responses to cell-damaging events. Nevertheless, PDI can become dysfunctional by post-translational modifications, including those promoted by biological oxidants. These oxidants are likely responsible for the oxidative post-translational modifications of PDI, which have detected under various conditions associated with oxidative stress, leading to protein dysfunction. However, the kinetics of the reactions of PDI with biological oxidants received limited studies and the products of these reactions were not characterized. Here, we examined whether the decrease in PDI fluorescence can be employed to follow the kinetics of the reaction of the full-length protein with biological oxidants. Also, we investigated the kinetics and products of the reaction between PDI and peroxynitrite. Our experiments showed that oxidation by excess hydrogen peroxide led to a decrease of PDI intrinsic fluorescence in a time- and concentration-dependent manner , permitting the determination of the second-order rate constant of the reaction (k = (17.3 ± 1.3 ) M1 s-1, pH 7.4, 25 ° C). The oxidation was reversed by DDT, indicating that hydrogen peroxide oxidizes mainly PDI dithiols (Cys53 and Cys56 and Cys397 and Cys400). Using the same approach to study PDI oxidation by peroxynitrite we noted that the decrease of the native PDI fluorescence was proportional to sub-stoichiometric or stoichiometric concentrations of the oxidant relative to that of PDI reactive thiols. Only under these conditions, PDI oxidation was reversed by DDT, indicating that PDI dithiols were the preferred target of peroxynitrite but that oxidation of other residues also occurred. The reaction of the active redox thiols of the PDI with peroxynitrite can be considered relatively fast (6.9 ± 0.6 × 104 M-1 s-1, pH 7.4, 25 ° C), and the reactive Cys residues of domains a and a\' were kinetically indistinguishable. Limited proteolysis experiments, kinetic simulations, and MS and MS/MS analyses confirmed that peroxynitrite preferentially oxidizes the redox-active Cys residues of PDI to the corresponding sulfenic acids, which subsequently react with the resolving thiols to produce disulfides (Cys53-Cys56 and Cys397-Cys400). However, a fraction of peroxynitrite decays to radicals leading to hydroxylation and nitration to other residues located close to the active site (Trp52 Trp396 and Tyr393). SDS-PAGE, western blotting and inhibition of the reductase activity experiments confirmed that excess peroxynitrite promotes further PDI oxidation, nitration, inactivation and aggregation in a concentration-dependent manner. MS and MS/MS analyzes showed that peroxynitrite in a ten times excess relative to PDI reactive thiols promote PDI nitration (Tyr43, Tyr49, Tyr196, Tyr393, Trp52, Trp396) and hydroxylation (Trp52, Trp396). In conclusion, our studies contribute to a better understanding of PDI oxidation by peroxynitrite and its possible biological consequences
Igbaria, Aeid. "Functional redox compartmentation of GSH in the yeast Saccharomyces cerevisiae." Thesis, Paris 11, 2011. http://www.theses.fr/2011PA112189.
Full textCys residue oxidation is a widespread biochemical modification occurring in all eukaryotic cells compartments. It serves oxidative protein folding in the endoplasmic reticulum (ER), protein import in the intermembrane space of mitochondria (IMS), and it has a regulatory role in the mitochondrial matrix and in the cytosol where it controls enzymes and signaling regulatory proteins activity. In all these processes, reversibility of Cys residue oxidation is a crucial feature. Two potent oxidoreductase systems, the glutathione (GSH) and thioredoxin pathways, catalyze disulfide bond reduction, and presumably control most thiol-redox-dependent cellular processes. However, despite tremendous knowledge of their enzymology, little is known about the physiological features of these systems in eukaryotes. To determine the physiologic importance of these functions and sort out which of them accounts for the GSH requirement for viability, we performed a comprehensive analysis of yeast cells depleted of or containing toxic levels of GSH. Both conditions triggered an intense iron-starvation-like response and impaired the activity of extra-mitochondrial ISC enzymes, but did not impact thiol-redox maintenance, except high glutathione levels that altered oxidative protein folding in the endoplasmic reticulum. While iron partially rescued the ISC maturation and growth defects of GSH-depleted cells, genetic experiments indicated that unlike thioredoxin, glutathione could not support by itself the thiolredox duties of the cell. We propose that glutathione is essential by its requirement in ISC assembly but only serves as a thioredoxin back up in cytosolic thiol-redox maintenance. Glutathione high physiologic levels are thus meant to insulate its function in iron metabolism from variations of its concentration during redox stresses, a model challenging the traditional view of it as prime actor in cytosolic thiol-redox control.Our preliminary data on the distribution of GSH inside cells collected by monitoring the redox state of rxYFP targeted to different cell compartments (ER, Matrix, Cytosol and IMS) in HGT1 cells indicate a specific transport of GSH into the ER and export of GSSG out of it. We were able to characterize two ABC transporters on which their deletion modify the redox state of the ER to more oxidizing and result in accumulation of higher GSSG content compared to WT. These data were confirmed by looking to the redox state of the PDI1 and ERO1 (WT and hyper active), all together suggest a role of these transporters in GSSG export from the ER, and that GSH flux between the different compartments is highly regulated
Norberg, Oscar. "Photochemical Ligation Techniques for Carbohydrate Biosensors and Protein Interaction Studies." Doctoral thesis, KTH, Organisk kemi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-90956.
Full textQC 20120309
Nguyen, Tuyet Mai. "Elucidation of thiol-protein oxidoreductase activity of the cytokine macrophage migration inhibitory factor (MIF) by biochemical redox and site-specific mutagenesis analysis." [S.l. : s.n.], 2003. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB10520514.
Full textAlegria, Thiago Geronimo Pires. "Caracterização cinética e busca de inibidores de Ohr (Organic Hydroperoxide Resistance protein) de Xylella fastidiosa." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/41/41131/tde-23072012-160418/.
Full textXylella fastidiosa is a gram-negative bacterium that colonizes the xylem and is the causative agent for several plant diseases. In Brazil, the main disease caused by this bacterium is the CVC (Citrus Variegated Chlorosis), which provokes large losses to the orange production in São Paulo and Minas Gerais states. Despite the current disease control, it has not been yet developed a specific method to eliminate the bacterium. During the plant-pathogen interactions, hosts produce an exacerbated amount of oxidants, in an attempt to eliminate the pathogen. Among them, fatty acids hydroperoxides are formed by the lipoxygenase action or even by the direct reaction between lipids and oxidant species. During the evolutionary process, pathogen defense mechanisms against oxidative species have evolved. Among them, Ohr (Organic Hydroperoxide Resistance protein) that is a Cys-based, lipoyl dependent peroxidase, displaying high activity towards organic hydroperoxides. This protein probably plays a central role in oxidative stress response and presnts some particularities, which make it a potential target for drug design. The objectives of this project were to characterize possible physiological substrates of Ohr from X. fastidiosa and search for molecules capable of inhibiting its peroxidase activity. Initially, we demonstrated that Ohr reduced fatty acid hydroperoxides with high efficiency (kcat/KM ~ 106 M-1.s-1). Moreover, these hydroperoxides inactivated Ohr in a dose-dependent manner, probably due to the high affinity between them and the enzyme. However, the enzyme did not display any activity towards phospholipids (posphatidilcholine) hydroperoxides and cholesterol hydroperoxide. Besides, we elucidated the structure of Ohr in the oxidized form (disulfide bond), which gave us insights on the dynamics of structural elements in the catalytic site. Ultimately, we identified a compound that was able to inhibit the peroxidase activity of Ohr in vitro, and we gained evidences that this compound can affect the bacterial growth under oxidative stress.
Siotto, Fenja [Verfasser], Thiel [Akademischer Betreuer] Thiel, and Adam [Akademischer Betreuer] Bertl. "Mining and analysis of new viral potassium channel proteins A structure and function study of new viral potassium channels from marine picoplankton and chlorella viruses / Fenja Siotto ; Thiel Thiel, Adam Bertl." Darmstadt : Universitäts- und Landesbibliothek Darmstadt, 2018. http://d-nb.info/1150400099/34.
Full textKohlstock, Ulf-Martin. "Protein C von Eubacterium acidaminophilum Sequenzanalyse und Funktion der Thiole von GrdD für die Freisetzung von Acetylphosphat /." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=963213261.
Full textZhang, Na. "Folding Analysis of Reduced Bovine Pancreatic Trypsin Inhibitor (BPTI) with Aromatic Thiols and Disulfides In Vitro." FIU Digital Commons, 2018. https://digitalcommons.fiu.edu/etd/3903.
Full textSabens, Elizabeth Ann. "Levodopa Drug Induced Alteration of Thiol Homeostasis in Model Neurons Activates Apoptosis Signaling Kinase 1: Implications for the Treatment of Parkinson's Disease." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1286464935.
Full textBernhard, Max [Verfasser], Gerhard [Akademischer Betreuer] Thiel, and Bodo [Akademischer Betreuer] Laube. "Binding Proteins and Receptor Binding Domains as Sensor Elements for Biological and Artificial Nanopores / Max Bernhard ; Gerhard Thiel, Bodo Laube." Darmstadt : Universitäts- und Landesbibliothek, 2021. http://d-nb.info/1236344782/34.
Full textRemelli, W. "FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS." Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/170507.
Full textBraun, Alexander. "The Interaction between a Thiol Specific Probe (OPA) and the Single Channel Characteristics of the Reconstituted Ca++ Release Protein from Skeletal Muscle Sarcoplasmic Reticulum." PDXScholar, 1995. https://pdxscholar.library.pdx.edu/open_access_etds/4869.
Full textAdigun, Risikat Ajibola. "Insight into the Reactivity of Metastasis Inhibitor, Imidazolium trans-[tetrachloro (dimethyl sulfoxide)(imidazole)ruthenate(III)], with Biologically-active Thiols." PDXScholar, 2012. https://pdxscholar.library.pdx.edu/open_access_etds/378.
Full textSassonia, Rogerio Corte. "Caracterização termodinamica de reações de nitrosação e interações proteicas por titulação calorimetrica isotermica." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/248521.
Full textTese (doutorado) - Universidade Estadual de Campinas, Instituto de Quimica
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Resumo: Este trabalho apresenta os resultados da aplicação da titulação calorimétrica isotérmica na caracterização termodinâmica de reações de S-nitrosação de tióis e de interações proteínaproteína e proteína-íon. Foram estudadas as reações de S-nitrosação da N-acetil-L-cisteína (NAC), L-cisteína (CYS), L-glutationa (GLU) e do ácido mercaptosuccínico. Também foram avaliadas as interações entre a proteína sinalizadora Shc (Src homology collagen-like) e as proteínas glutationa S-transferase (GST) e a ciclofilina A (CypA) e a interação entre a região Cterminal da proteína humana EFHC1 (EFHC1-C) com íons Ca e Mg. Os valores da variação de entalpia revelaram que a S-nitrosação é um fenômeno exotérmico e ocorre com diminuição de entropia. Estes dados termodinâmicos revelam que as reações de S-nitrosação investigadas são entalpicamente dirigidas a 25 °C (1 atm) e possuem valores semelhantes de variações de entalpia, entropia e energia livre, apesar das diferenças entre as estruturas químicas dos tióis. Verificou-se que a proteína EFHC1C liga-se tanto a íons Ca quanto Mg numa estequiometria de 1:1, com afinidades definidas por diferentes contribuições entálpicas e entrópicas. Este dado confirmou a existência de um suposto domínio EF-hand ligante de Ca na porção C-terminal previsto pela seqüência primária da EFHC1C. Por outro lado, a EFHC1C perde sua capacidade de interação com íons Ca e Mg em solução sem 1,4-ditiotreitol (DTT), provavelmente, devido à formação de dímeros. A ausência de sinais térmicos de ITC mostrou que nem a proteína GST, nem a proteína CypA interagem com a proteína Shc nas condições experimentais usadas.
Abstract: This work presents the results of isothermal titration calorimetry application in the thermodynamic characterization of thiol nitrosation reactions, protein-protein and protein-ion interactions. The S-nitrosation reactions of N-acetyl-L-cysteine (NAC), L-cysteine (CYS), Lglutathione (GLU) and acid mercaptosuccinic were studied. The interactions of the signaling protein Shc (Src homology collagen-like) with glutathione S-transferase (GST) and ciclofilina A (CypA) and of the EF-hand motif from human EFHC1C with Caand Mg ions were also evaluated. Enthalpy change values revealed that the S-nitrosation reaction is an exothermic phenomenum associated to a decrease in entropy. These thermodynamic data show that the S-nitrosation reactions investigated are enthalpically driven at 25 °C (1 atm) and have similar enthalpic, entropic and free energy change values, despite the differences among the chemical structures of the thiols. It was verified that the EFHC1C protein binds to both Ca and Mg ions in a 1:1 stoichiometry with affinities defined by different enthalpic and entropic contributions. These data confirmed the presence of a putative EF-hand Ca-binding motif at the C-terminal portion as expected by the primary sequence of EFHC1C. On the other hand, EFHC1C losses its ability to interact with Ca and Mgions in solution without 1,4-ditiotreitol (DTT) likely due to protein dimerization. The absence of ITC thermal signals showed that neither GST nor CypA interact with the Shc protein in the experimental conditions used.
Doutorado
Físico-Química
Doutor em Ciências
Cussiol, José Renato Rosa. "Caracterização funcional de uma nova proteína antioxidante: Ohr (Organic Hydroperoxide Resistance Protein). Vias de redução e expressão em Xylella fastidiosa." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/41/41131/tde-21072010-161740/.
Full textXylella fastidiosa is a gram-negative bacterium, which colonizes the xylem from economically important plants, being responsible for several diseases such as Pierce disease (PD) in gravepines and citrus variegated clorosis (CVC). Plants, when infected by pathogens, are able to defend themselves through several mechanisms which include the generation of reactive oxygen species (ROS). Lipid hydroperoxides can be generated from the attack of ROS to the bacterial membrane or by the action of lipoxygenases. The alkyl hydroperoxide reductase system (AhpR) was initially characterized as the main responsible for the detoxification of organic hydroperoxides in bacteria. Recently, it was also characterized another gene in many pathogenic bacteria, whose deletion renders cells susceptibility to organic hydroperoxide treatments but not by H2O2 or by superoxide generators (Mongkolsuk et al., 1998 and Ochsner et al., 2001). For this reason, it was named ohr (organic hydroperoxide resistance gene). The goal of this work was to functionally characterize ohr, the product of ohr gene from Xylella fastidiosa. Initially, we demonstrated that ohr possesses Cys-based thiol-dependent peroxidase activity. Later, we showed that ohr possesses a unique alpha/beta fold not observed in the structures of other thiol peroxidases such as peroxiredoxins and glutathione peroxidases. Analyses of ohr active site showed that its likely substrates are elongated and hydrophobic molecules. Furthermore, we showed that lipoylated enzymes, classically related with the intermediary metabolism, interacts physically and functionally with ohr while classical thiol-dependent pathways, such as thioredoxin and glutathione, failed to support ohr activity. This finding represents the first evidence of a peroxidase that is directly reduced by lipoyl groups of enzymes. Also, we obtained evidences indicating that ohr acts in the detoxification of peroxides derived from unsaturated fatty acids. In fact, steady-state kinetics using bi-substrate analysis showed that ohr decomposes organic peroxides with high efficiency (kcat/KM ~ 106 M-1.s-1 through a ping-pong mechanism, at least ten thousand times more efficiently than hydrogen peroxide (H2O2). All these results together shows that ohr is central in the response of bacteria to the stress induced by organic hydroperoxides but not by H2O2 and defines a new class of antioxidant enzymes with unique properties such as lipoyl-dependent peroxidase activity. Another goal of this work was to study the regulation of ohr expression in Xylella fastidiosa. ohr expression is regulated in most bacteria by a repressor protein named ohrR (Sukchawalit et al., 2001) but, in some bacteria, ohr expression is positively regulated by an alternative sigma factor (σE) with extracitoplasmatic function (Gourion et al., 2008). Our results showed that ohr from X. fastidiosa was not under the control of none of these regulators, probably being constitutively expressed. Through northern blot analysis, we did not observed any changes in ohr levels in cells submitted to oxidative or ethanolic stress. These results, indicates that ohr expression probably differs from that previously described on literature for other bacteria.
Larsson, Rikard. "Dynamic Systems for Screening, Control and Identification of Protein-Ligand Interactions." Doctoral thesis, Stockholm : Kemi, Chemistry, Kungliga Tekniska högskolan, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4709.
Full textDomingos, Renato Mateus. "Conserved structural and dynamic aspects behind Ohr enzymatic catalysis: Ohr as potential drug targets." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/41/41131/tde-07032019-090053/.
Full textAs proteínas Ohr (Organic hydroperoxide resistance) são peroxidases dependente de tiól extremamente eficientes e têm um papel central na resposta das bactérias contra peróxidos orgânicos. Em fungos, as proteínas Ohr apresentam uma extensão N-terminal, cujo predições in silico apontam estar associada ao direcionamento da proteína para a mitocôndria. A tríade catalítica é composta pela cisteína peroxidatic (Cp), a arginina (Rc) e o glutamato (Ec) catalíticos que são totalmente conservados e interagem entre eles por uma rede de interações de ponte salina, na forma reduzida da proteína (conformação fechada). Após se tornarem oxidadas em ácido sulfênico (Cis-SOH), a Cp condensa com o grupo sulfidrila da cisteína de resolução (Cr) numa ligação disulfeto. A ausência da carga negativa do tiolato (RS-) da Cp facilita a abertura da alça que contem a Rc para longe do centro ativo, gerando a conformação aberta. No entanto, os eventos moleculares associados a alta reatividade das enzimas Ohr contra hidroperóxidos e a sua redução pela dihydrolipoamida (presente em proteínas lipoiladas), ainda está descrita de forma bem superficial. Adicionalmente, vários fatores suportam a ideia de que a Ohr seria um potencial alvo para o desenvolvimento de drogas: (i) a Ohr exibe propriedade físico-químicas únicas; (ii) as bactérias mutantes para Ohr (Δohr) são fortemente sensíveis ao stress oxidativo; (iii) indicações de que a Ohr poderá está envolvida na virulência de várias bactérias; e (iv) a ausência de Ohr em mamíferos e plantas vascularizadas. Nesta tese, vários aspetos relacionados com as enzimas Ohr foram avaliados. No Capitulo 2, foi caracterizada bioquimicamente a proteína Ohr homologa de fungo ascomiceto, Mycosphaerella fijiensis Mf_1 (MfOhr), o agente causador da doença de bananas, Sigatoka-negra. A enzima apresentou eficiente atividade contra peroxido de ácido linoleico (kobs = 3.18 (± 2.13) ×108 M-1.s-1). Além disso, através do fracionamento sub celular de protoblasto de M fijiensis seguido de western blot, foram confirmadas as predições in silico de que a MfOhr é uma proteína mitocondrial. No capítulo 3 e 4, foram descritas sete estruturas cristalográficas oriundas de dois patógenos oportunistas, uma de Xylella fastidiosa e seis de Chromobacterium violaceum (incluindo o primeiro representante do complexo entre a Ohr e o seu redutor biológico, DHL). Estas estruturas poderão representar diferentes conformações ao longo do ciclo catalítico. Adicionalmente, várias abordagens de modelagem molecular, tais como mecânica clássica (MM), mecânica molecular direcionada (SMM) e mecânica quântica híbrida (QM-MM), juntamente com ensaios experimentais com mutações pontuais, indicaram que a Ohr sofre várias mudanças conformacionais para permitir uma abertura intermitente (estado oxidado) e o retorno para uma conformação fechada mais estável (estado reduzido) da alça da arginina ao longo da catálise. Notavelmente, a dihydrolipoamide assistiu diretamente o fechamento da alça da arginina e por consequência o turnover da enzima. No capítulo 5, foi descrita a identificação de dois compostos (C-31 e C-42) que representam estudos iniciais com a finalidade de encontrar inibidores específicos para a enzima Ohr. Estes compostos foram encontrados por ab initio design e por varrimento virtual com o uso de modelos farmacofóricos. Os IC50 calculados para o C-31 e C-42 foram de 124.4-248.5 µM e 243.3-321.7 µM, respectivamente. Finalmente, esta tese descreve vários aspetos relacionados com a função da Ohr: 1 - evidências que as Ohr de eucariotos estão preferencialmente localizadas na mitocôndria e partilham várias propriedades bioquímicas com as Ohr de bactéria; 2 - a rede de interações polares entre os resíduos da tríade catalítica (Cp, Rc e Ec) contribuem fortemente para a estabilização do estado fechado, a configuração ótima para a redução de hydroperoxidos; 3 - evidências de que a formação da ligação disulfeto e a liberação do produto (álcool derivado da redução do hydroperoxido) facilitam a abertura da alça da arginina até um estado intermediários (provavelmente não o estado totalmente exposto apresentado nas estruturas cristalográficas) 4 - o mapeamento das interações entre o redutor biológico no centro ativo da Ohr; 5 - fortes indicações de que a DHL não é capaz de interagir e reagir com a Ohr na conformação fechada; 6 - os primeiros ensaios para a procura por moléculas que especificamente interajam com a Ohr, apesar de que futuros ensaios terão de ser executados para verificar a especificidade dos compostos selecionados. Assim, nós descrevemos nova informação relevante sobre uma proteína antioxidante que exibe uma alta eficiência catalítica, comparável com outras importantes enzimas removedores de hydroperoxidos, tais como glutationa peroxidases e peroxiredoxinas
Voigt, Christin [Verfasser], H. Ulrich [Akademischer Betreuer] Göringer, and Gerhard [Akademischer Betreuer] Thiel. "Surface-Driven RNA Refolding by the OB-Fold Proteins of the Trypanosoma brucei Editosome / Christin Voigt ; H. Ulrich Göringer, Gerhard Thiel." Darmstadt : Universitäts- und Landesbibliothek Darmstadt, 2017. http://d-nb.info/1131254244/34.
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