Дисертації з теми "Outer membrane protein A (OmpA)"
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Kaye, Elena Cortizas. "The Function of Outer Membrane Protein A (OmpA) in Yersinia pestis." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_theses/58.
Повний текст джерелаSchesser, Bartra Sara Celinda. "Outer membrane proteins of Yersinia pestis : Ail and OmpA." Doctoral thesis, Umeå universitet, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet), 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-33956.
Повний текст джерелаAl-Akash, Ahmed M. "Increased expression of ompA, ompX, dedA, and gutS genes in Enterobacter sp. YSU in the presence of selenite." Youngstown State University / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1607517925584702.
Повний текст джерелаMcCallan, Lyanne Mary. "Differentiation of Campylobacter jejuni on the basis of outer membrane protein (OMP) patterns." Thesis, University of Ulster, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422191.
Повний текст джерелаGerlach, Lisa [Verfasser]. "BamB facilitates folding of outer membrane protein A (OmpA) via interactions of its β-propeller with the membrane surface and via a conformation change induced by phosphatidylglycerol / Lisa Gerlach". Kassel : Universitätsbibliothek Kassel, 2020. http://d-nb.info/1204016488/34.
Повний текст джерелаKevin, Gross. "Characterization of a fourU RNA thermometer in the ompA gene of Shigella dysenteriae." Ohio University Honors Tutorial College / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=ouhonors1367582905.
Повний текст джерелаDahlstrand, Rudin Arvid, and John Burstedt. "The importance of OuterMembrane Protein A in SerumResistance in Aggregatibacteractinomycetemcomitans serotype astrain D7SS." Thesis, Umeå universitet, Institutionen för odontologi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-143904.
Повний текст джерелаEaston, Donna Meredith, and n/a. "Functional and Antigenic Characterisation of the Moraxella catarrhalis protein M35." University of Canberra. n/a, 2008. http://erl.canberra.edu.au./public/adt-AUC20081217.083105.
Повний текст джерелаLi, Huanyu. "Structural studies of the BAM complex, OmpU outer membrane protein and lipoprotein N-acyl transferase in Gram-negative bacteria." Thesis, University of East Anglia, 2017. https://ueaeprints.uea.ac.uk/68718/.
Повний текст джерелаHolmqvist, Erik. "Macromolecular Matchmaking : Mechanisms and Biology of Bacterial Small RNAs." Doctoral thesis, Uppsala universitet, Mikrobiologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-171642.
Повний текст джерелаThotakura, Gangadaar. "Structural prediction analysis of ehrlichia chaffeensis outer membrane proteins, p28 Omp-14 and p28 Omp-19 assessed by circular dichrosim and porin assays." Thesis, Kansas State University, 2011. http://hdl.handle.net/2097/9098.
Повний текст джерелаDepartment of Diagnostic Medicine/Pathobiology
Roman Reddy R. Ganta
Ehrlichia chaffeensis, a Gram-negative organism belonging to the order Rickettsiales, is responsible for an emerging infectious disease in humans, the human monocytic ehrlichiosis. E. chaffeensis also infects several other vertebrate hosts including dogs, goats, coyotes and white tailed deers. This organism is transmitted by an infected tick, Amblyomma americanum. The exact pathogenic mechanisms involved for the persistence of the pathogen in vertebrate hosts are still unclear. E. chaffeensis protein expression varies significantly in vertebrate and tick hosts. Differentially expressed proteins include the immunodominant outer membrane proteins encoded by the p28-Omp multigene locus. The p28-Omp 14 is expressed primarily in tick cells and the p28-Omp 19 is the major expressed protein in macrophages both under in vitro and in vivo conditions. The objective of this study is to prepare recombinant proteins and use them to assess the secondary structures and protein functions. The protein sequences were analyzed with the aid of bioinformatics programs to make structural predictions. The analysis suggested the presence of eight β barrel structures for both the p28-Omp proteins. The coding sequence of the p28-Omp genes were cloned and over expressions of proteins in in E. coli was accomplished by using the plasmid expression construct, pET28. The proteins were purified to near homogeneity and used to refold using detergents to mimic native protein structure in the bacterial outer membrane. Refolding of proteins was analyzed by two methods; SDS-PAGE and Circular Dichroism. The Circular dichroism spectroscopy analysis suggested the formation of β-sheet structures of proteins in micelles formed with the detergents. β-sheet structures may have been formed with the hydrophobic domains of the protein imbedded in the micelles. The hydrophilic segments (predicted by bio informatics analysis) may be exposed to the aqueous phase. The recombinant proteins were also iii used to prepare proteoliposomes and tested for the porin activity. The analysis demonstrated the porin activity for both p28-Omp 14 and 19 recombinant proteins by using mono-, di- and tetra- saccharides as well as for amino acid L-glutamine. This study forms the basis for initiating studies to compare the structural difference between the two differentially expressed proteins of E. chaffeensis.
Barlow, Ann Katherine. "Neisseria meningitidis : the class 1 outer membrane protein." Thesis, University of Southampton, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.280415.
Повний текст джерелаMcBride, Heidi May. "Protein import into and across the mitochondrial outer membrane." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40395.
Повний текст джерелаConsistent with this model, the signal-anchor sequence of the outer membrane protein yTom70 is also capable of importing into the inner membrane of mitochondria when the outer membrane is selectively removed. Import into the inner membrane requires the presence of an electrochemical potential across the lipid bilayer. Import proceeds in the absence of $ Delta Psi$ only when constructs are used which lack the positively-charged amino terminal region of the signal-anchor sequence. These results suggest that the positively-charged presequence leads the transmembrane domain into the import machinery and that $ Delta Psi$ is required to clear this region in order that the distal transmembrane region can enter the translocation pathway.
The charged N-terminal 10 residues of yTom70 are incapable of directing import into intact mammalian mitochondria, however, are able to efficiently direct import into the matrix of yeast mitochondria or mammalian mitoplasts. This potentially cryptic signal is excluded from intact mammalian mitochondria due to the presence of the receptor protein Tom20, since replacement of yeast Tom20 with mammalian Tom20 confers the mammalian phenotype onto yeast. These results suggest that receptor proteins may also have the ability to screen potentially cryptic signals from distal components of the outer and inner membrane translocation machinery.
Menon, Sailesh. "Characterization of a Fusobacterium necrophorum subspecies necrophorum outer membrane protein." Kansas State University, 2014. http://hdl.handle.net/2097/18128.
Повний текст джерелаDepartment of Biomedical Sciences
Sanjeev K. Narayanan
Fusobacterium necrophorum is an anaerobic Gram-negative non spore forming rod shaped bacteria that is a normal inhabitant of the alimentary tract of humans and animals. Two subspecies of F. necrophorum have been recognized- subspecies necrophorum and subspecies funduliforme. Subspecies necrophorum is an opportunistic pathogen in animals causing diseases such as bovine hepatic abscesses and sheep foot rot while as subspecies funduliforme is linked with human oral and hepatic infections such as sore throats, Lemierre’s syndrome and hepatic abscesses. The pathogenic mechanisms of F. necrophorum are complex and are not well understood or defined. Several virulence factors such as leukotoxin, haemolysin, haemagglutinin and adhesin have been described. One of the most important factors in F. necrophorum bacterial pathogenesis is the adhesion of the bacteria to the host cell. The adhesion of the bacteria to the host cell helps it colonize the host tissue and this is followed by intracellular multiplication with dissemination to other tissues, which could ultimately lead to septicemia and death. Bacteria use adhesins which are proteins found in the outer membrane which help them bind with host receptors and this helps with the adhesion of the bacteria to the host cell. Not much is known about F. necrophorum adhesins. Here, we describe and characterize a novel adhesin.
Shand, Geoffrey H. "Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginosa." Thesis, Aston University, 1985. http://publications.aston.ac.uk/12475/.
Повний текст джерелаSanchez, Katheryn Marie. "Ultraviolet resonance Raman and fluorescence studies of folded and unfolded conformations of the membrane protein OmpA." Diss., [La Jolla] : University of California, San Diego, 2010. http://wwwlib.umi.com/cr/ucsd/fullcit?p3397317.
Повний текст джерелаTitle from first page of PDF file (viewed April 7, 2010). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
See, Sarah Bihui. "Outer membrane protein immunity to Pasteurella pneumotropica and the interaction of allergy." University of Western Australia. School of Paediatrics and Child Health, 2010. http://theses.library.uwa.edu.au/adt-WU2010.0103.
Повний текст джерелаFerris, Shirley. "Antibody responses to the major outer membrane protein of Chlamydia trachomatis." Thesis, University of Southampton, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295880.
Повний текст джерелаSchiffrin, Robert. "Roles of periplasmic chaperones and BamA in outer membrane protein folding." Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15952/.
Повний текст джерелаHuysmans, Gerard Herman Marleen. "On the folding mechanism of the bacterial outer membrane protein PagP." Thesis, University of Leeds, 2008. http://etheses.whiterose.ac.uk/6752/.
Повний текст джерелаWebb, Dianne, and n/a. "Nontypeable Haemophilus influenzae outer membrane protein analysis, isolation, characterisation and vaccine potential." University of Canberra. Applied Science, 1998. http://erl.canberra.edu.au./public/adt-AUC20061110.105953.
Повний текст джерелаArbing, Mark A. "Electrophysiological properties of porin, the major outer membrane protein of Haemophilus influenzae." Thesis, McGill University, 2002. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=38146.
Повний текст джерелаTo study the properties of the porin (341 amino acids; Mr 37,782) of Haemophilus influenzae type b (Hib), purified porin was subjected to chemical modification. The covalent modification of lysine residues with succinic anhydride (SA; Mr 100.08) results in charge reversal. The addition of up to 12 succinate groups per porin molecule was identified using electrospray ionization mass spectrometry (MS). Tryptic digestion of the modified Hib porin followed by reverse phase chromatography and matrix assisted laser desorption ionization time-of-flight MS identified the sites of succinylation. The majority of modified lysines were positioned in surface-located loops, numbers 1 and 4 to 7. When the electrophysiological properties of SA-modified porin were analyzed in planar lipid bilayers (PLBs) and compared to Hib porin it was found that the single channel conductance was increased, while the threshold for voltage gating was decreased. The addition of extra negative charges increase the single channel conductance of Hib porin and function as voltage sensors.
Selected lysine residues that were found to be modified with SA were substituted with glutamic acid using site-directed mutagenesis. Single point mutations were made in a residue assigned to the barrel lumen and to three residues in each of loops 4 and 6. The mutant Hib porins had increased single channel conductances relative to wild-type Hib porin. Voltage gating of mutant Hib porins was altered by the introduction of negative charges into loops 4 and 6 and in the barrel lumen. Previous experiments had implicated surface-exposed loop 4 in voltage gating. This study ascribes a role for residues in loop 6 and a residue within the barrel lumen in the changes that accompany pore closure.
Hi strains causing infection in cystic fibrosis patients are capable of persistent infection despite prolonged antibiotic treatment with beta-lactam antibiotics. During the course of infection porin properties may be altered due to the changes in porin sequences that are attributed to antigenic drift. The electrophysiological properties of four porins from CF patient-derived Hi strains were characterized to examine changes in porin properties arising from persistent infection of the CF lung. The clinical Hi porins displayed altered channel properties that included increased voltage sensitivity and single channel conductances that were either greater or smaller than that of Hib porin. The decreased single channel conductance of one of the porins was associated with an increase in the minimal inhibitory concentration of the antibiotics novobiocin and streptomycin. These results demonstrate a porin-mediated decrease in OM permeability as an antibiotic resistance mechanism for Hi.
Carter, Michael William. "The major outer membrane protein gene of Chlamydia as a phylogenetic chronometer." Thesis, University of Southampton, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.336071.
Повний текст джерелаEneroth, Elina, and Astrid Karlsson. "A role of Aggregatibacter actinomycetemcomitans Outer Membrane Protein 100 in Serum Resistance?" Thesis, Umeå universitet, Institutionen för odontologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-128759.
Повний текст джерелаMorgan, Cecilia A. "Treponema pallidum repeat protein K and heterologous protection against syphilis /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/9300.
Повний текст джерелаOliveira-Fry, Anna Maria, and s9911120@student rmit edu au. "Identification of Legionella outer membrane proteins for the development of a biosensor." RMIT University. Applied Sciences, 2007. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080513.140744.
Повний текст джерелаDahan, David. "Biophysics of porin, the major outer membrane protein of Haemophilus influenzae type b." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0025/NQ29916.pdf.
Повний текст джерелаSrikumar, Ramakrishnan. "Topology of porin, the major outer membrane protein of Haemophilus influenzae type b." Thesis, McGill University, 1995. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40261.
Повний текст джерелаBased on parameters of hydrophilicity and amphiphilicity a model for Hib porin was generated. The model proposed an organization of sixteen anti-parallel $ beta$-strands that traverse the outer membrane, eight long loops that connect the $ beta$-strands on one side and short turns on the other side.
By flow cytometry, six out of a panel of nine monoclonal antibodies against Hib porin recognized amino acid sequences at the cell surface. Hib porin was purified and subjected to chemical and enzymatic digestions. The fragments were immunoblotted; N-terminal sequencing identified boundaries of fragments. C-terminal deletions of Hib porin generated in the baculovirus expression system identified C-terminal boundaries of monoclonal antibody reactivities.
To map precisely the primary sequences to which these monoclonal antibodies bound, overlapping hexapeptides for the entire sequence of Hib porin were synthesized. These studies identified two surface-exposed regions in the mature sequence of Hib porin, amino acid residues 162-172 and 318-325. In the Hib porin model, these regions correspond to loops 4 and 8, respectively. Two regions between residues 112-126 (loop 3) and residues 148-153 were buried or inaccessible at the surface of the outer membrane.
Recombinant Hib porin was expressed in Bacillus subtilis. The biophysical and immunological properties of this lipooligosaccharide-free recombinant Hib porin were compared with those of native Hib porin.
In order to examine the role of loop 3, site-directed mutagenesis of the cloned Hib porin gene was undertaken. Six or twelve amino acid deletions in loop 3, expressed in a porin deletion strain, showed significant increase in sensitivities to several anti-microbial agents as compared to wild-type Hib porin. Deletion of twelve amino acids showed more pronounced phenotypes than deletion of six amino acids. Such mutagenesis experiments provided support to the notion that loop 3 in Hib porin folds back into the pore and produces a constriction of the channel.
Dahan, David. "Biophysics of porin : the major outer membrane protein of Haemophilus influenzae type b." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=42009.
Повний текст джерелаBased on predictions of porin secondary structure, a model of Hib porin was generated. The model proposed sixteen membrane spanning $ beta$-strands connected by eight long loops on one side and eight short $ beta$-turns on the other side. To refine further this model, the epitopes of nine monoclonal antibodies specific for Hib porin were mapped precisely. Surface-exposure of these epitopes was determined by flow cytometry of intact Hib cells. Our studies identified two surface-exposed regions of Hib porin: amino acids 162 to 172, and 318 to 325. These two regions correspond to loops 4 and 8 in the Hib porin model.
Three naturally occurring Hib porin variants were purified, reconstituted into planar bilayers, and analyzed for their voltage dependency. Substitutions at Arg166 residue, which is localized to loop 4, were associated with a lowered threshold potential for the voltage gating of Hib porin. This surface-exposed loop was therefore implicated in the conformational changes that are postulated to occur during voltage gating.
Lipooligosaccharide (LOS) binds tightly to Hib porin. To generate large amounts of Hib porin devoid of LOS, the ompP2 gene was cloned into an expression vector of Bacillus subtilis. Recombinant Hib porin was produced in large quantities and it aggregated into inclusion bodies. Under denaturing conditions, recombinant porin was purified to homogeneity and subsequently refolded. To assess the fidelity of refolding of recombinant porin, four criteria were used: spectroscopic properties, channel formation in planar bilayers, resistance to trypsin digestion and formation of the conformational epitope recognized by monoclonal antibody Hb-2. We conclude that in the absence of LOS, recombinant porin was refolded into a functional form, its structure closely resembling the native state.
Ward, Stephen John. "Characterisation and immunogenicity of recombinant class 1 outer membrane protein of Neisseria meningitidis." Thesis, University of Southampton, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296140.
Повний текст джерелаHuang, Shouxiong. "Genetic and Antigenic Characterization of the Major Outer Membrane Protein of Campylobacter Jejuni." The Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=osu1046991783.
Повний текст джерелаWyllie, Susan. "Structural and functional characterisation of the major outer membrane protein of Chlamydia psittaci." Thesis, University of Edinburgh, 1999. http://hdl.handle.net/1842/22762.
Повний текст джерелаAguilar, Mónica Alejandra Pavez. "Caracterização molecular da resistência aos carbapenêmicos em enterobactérias isoladas em hospitais brasileiros." Universidade de São Paulo, 2009. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-28092009-144325/.
Повний текст джерелаIntroduction: After emergence, and dissemination of extended spectrum β-lactamases (ESBL) in members of the Enterobacteriaceae family, carbapenem antibiotics (imipenem, meropenem, ertapenem) have been the therapy of choice, since they are stable to ESBL hydrolysis. Unfortunately, in 2005, the first fatal case of infection by carbapenem-resistant Klebsiella pneumoniae was related in our country. From this episode, new infection cases, including by other genders of Enterobacteriaceae such as Enterobacter, Providencia and Escherichia, began to appear. Regarding carbapenem resistance mechanisms, expression of carbapenem hydrolyzing enzymes has been worldwide reported, whereas interplay between impermeability and AmpC or ESBL production has been sporadic. Furthermore, integrons and plasmids have been associated with mobilization of genetic determinants. The aim of this study was to characterize the mechanisms of resistance to carbapenems, their genetic mobilization and clonal dissemination in enterobacterial isolates recovered from clinical samples in Brazilian hospitals. Material and methods: 28 imipenem-resistant isolates recovered from 8 hospital centres were studied. Phenotypic profiles were characterized by: i) MIC of carbapenems in the presence/absence of β-lactamase inhibitors; ii) bioassay for β-lactamase production; iii) SDS-PAGE to investigate absence of outer membrane porins (OMPs). Molecular characterization of β-lactamase-mediated resistance was made by PCR and DNA sequencing and their plasmid localization was evaluated by transformation. Finally, epidemiological typing was performed by ERIC-PCR, being confirmed by PFGE. Results: 25 isolates were confirmed as being resistant to imipenem (MIC 8-128 µg/mL), exhibiting a multidrug-resistant profile, including to cefoxitin (MIC90 ≥32 µg/mL). Two main mechanism of resistance were identified: i) hydrolysis of carbapenem by class B (IMP-1-like MBL) and class A (KPC-2) enzymes, (the latter being recently reported in our country), and ii) outer membrane impermeability associated to AmpC enzyme production (plasmid-mediated CMY-2 for E. coli and chromosomal AmpC for E. aerogenes), which was the most prevalent mechanism found. Eighteen of 28 isolates lacked 36kDa OMP, which is responsible for uptake of carbapenem antibiotics. The blaKPC-2 and blaCMY-2 genes were successful transferred to E. coli DH10B, confirming the plasmid location of both genes. Co-production of carbapenemases or AmpC and CTXM enzymes was confirmed in 68% of isolates, and molecular typing showed clonal dissemination of IMP-1-, plasmid AmpC- and chromosomal AmpC-producing isolates. Otherwise, KPC-2-producing isolates were not clonally related. Conclusion: The characterization of resistance mechanisms to carbapenems, in this study, reveals a change in the resistance patterns among Enterobacteriaceae family members in Brazilian hospitals, due to versatility of isolates to acquire new resistance determinants, which it has favoured the adaptation to hostile environments. Lack of 36 kDa OMP was the most frequent resistance mechanism, being associated to co-production of β-lactamases. Finally, molecular typing denote a clonal dissemination of imipenem-resistant isolates in Sao Paulo city, with exception of KPC-2-producing isolates, which have been described in other Brazilian cities, suggesting a horizontal gene transfer.
Neary, Tiffany Jonean. "Ultraviolet resonance Raman spectroscopy of the integral membrane protein OmpA elucidating structure and tryptophan microenvironment of folded and unfolded states /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p1459291.
Повний текст джерелаTitle from first page of PDF file (viewed November 13, 2008). Available via ProQuest Digital Dissertations. Includes bibliographical references.
McGuinness, Brian Timothy. "Immunochemistry and structural variation of the class 1 outer membrane protein of Neisseria meningitidis." Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386663.
Повний текст джерелаHumes, Julia Rose. "The mechanism of the ATP-independent periplasmic chaperone SurA in outer membrane protein biogenesis." Thesis, University of Leeds, 2018. http://etheses.whiterose.ac.uk/22526/.
Повний текст джерелаMcMorran, Lindsay Madeline. "Mechanisms of outer membrane protein folding : effects of the lipid environment and periplasmic chaperones." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/5906/.
Повний текст джерелаJuodeikis, Rokas. "Engineering membranes in Escherichia coli : the magnetosome, LemA protein family and outer membrane vesicles." Thesis, University of Kent, 2016. https://kar.kent.ac.uk/61062/.
Повний текст джерелаau, T. La@murdoch edu, and Tom La. "Characterisation, Recombinant Expression and Immunogenicity of BHLP29.7, An Outer Membrane Lipoprotein of Brachyspira Hyodysenteriae." Murdoch University, 2006. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20070830.141953.
Повний текст джерелаRios, Rosa Elvira. "Characterisation of the physiological, chemical and pathogenic changes arising from the adaptation of Campylobacter jejuni to aerotolerant growth." Thesis, Manchester Metropolitan University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243715.
Повний текст джерелаFischer, Steven Harold. "Interactions of Neisseria gonorrhoeae with human neutrophils: Gonococcal outer membrane protein II modulates neutrophil responses." Diss., The University of Arizona, 1988. http://hdl.handle.net/10150/184364.
Повний текст джерелаSukumaran, Suja. "Spectroscopic investigation of stability, unfolding and refolding of outer membrane protein porin from Paracoccus denitrificans." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=974953849.
Повний текст джерелаBell, Angus. "Structure, function, and role in antibiotic resistance of outer membrane protein H1 in Pseudomonas aeruginosa." Thesis, University of British Columbia, 1989. http://hdl.handle.net/2429/29008.
Повний текст джерелаScience, Faculty of
Microbiology and Immunology, Department of
Graduate
Berry, Jody Douglas. "Antibody gene markers and their relationship to chlamydial major outer membrane protein (MOMP) immune response." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0006/NQ41602.pdf.
Повний текст джерелаButt, Neil James. "The complete nucleotide sequence and immunochemistry of the major outer membrane protein of Neisseria gonorrhoeae." Thesis, University of Southampton, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.316059.
Повний текст джерелаBulieris, Paula Vasilichia. "Kinetic Studies on the Folding and Insertion of Outer Membrane Protein A from Escherichia Coli." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-48784.
Повний текст джерелаUjwal, Rachma. "Structural and fuctional characterization of the outer mitochondrial membrane protein voltage-dependent anion channel 1/." Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1930281371&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.
Повний текст джерелаKöniger, Verena [Verfasser], and Rainer [Akademischer Betreuer] Haas. "CEACAMs as novel receptors for Helicobacter pylori outer membrane protein HopQ / Verena Königer ; Betreuer: Rainer Haas." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2016. http://d-nb.info/1119073731/34.
Повний текст джерелаKhursigara, Cezar M. "Interactions between the energy-transducing protein TonB and the outer membrane receptor FhuA from Escherichia coli." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=85563.
Повний текст джерелаSedimentation velocity analytical ultracentrifugation (AUC) experiments involving mixtures of recombinant TonB and FhuA were conducted to determine the oligomeric state of TonB-FhuA complexes. These experiments demonstrated that wild-type TonB-FhuA proteins form a 2:1 (TonB:FhuA) complex, and that this complex is more abundant when FhuA is pre-incubated with the siderophore Fc. Deletion of the N-terminal region of TonB also demonstrated a 2:1 complex stoichiometry with FhuA, but in much lower abundance. Deletion of a highly conserved proline-rich region within TonB resulted in the formation of a 1:1 complex, suggesting a novel role for this domain in the formation of a functional 2:1 complex.
Affinities of interaction between wild-type and mutant TonB and FhuA proteins were measured by surface plasmon resonance (SPR). SPR data revealed that wild-type TonB-FhuA interactions are comprised of multiple interaction sites, and undergo an intermediate rearrangement event prior to the formation of the 2:1 complex. Deletions of TonB domains do not disrupt this rearrangement, but do decrease affinity. FhuA cork domain deletions also identified novel sites important for stable interactions.
Information of TonB-FhuA interactions derived by AUC and SPR described herein has contributed greatly to the purification and crystallization of TonB-FhuA co-complexes. Overall, these complementary biophysical techniques have provided important mechanistic details into the protein-mediated transport of iron into Gram-negative bacteria, and will provide a conceptual framework of TonB-FhuA that will help in elucidating aspects of the high-resolution structure of the complex.
Malia, Thomas J. 1977. "NMR structural and functional studies of the mithochondrial outer membrane protein VDAC by Thomas J. Malia." Thesis, Massachusetts Institute of Technology, 2006. http://hdl.handle.net/1721.1/37889.
Повний текст джерела"September 2006." Vita.
Includes bibliographical references.
Apoptosis is a mechanism of programmed cell death required by multicellular organisms during development and for tissue maintenance. Bcl-2 family proteins are central regulators of apoptosis and many of their primary roles are carried out in the outer mitochondrial membrane. Anti-apoptotic Bcl-xL has been found previously to interact with VDAC, an outer mitochondrial membrane protein responsible for metabolite trafficking. Here, the NMR-based investigation of VDAC and its interaction with Bcl-xL in detergent micelles is described. As an integral membrane protein VDAC presented a challenge for producing a folded form amenable to solution NMR studies. Methods developed for expression and purification of human VDAC for structural studies by NMR spectroscopy were developed. Optimal sample conditions were explored in a screen of various detergents and buffers. Suitable NMR sample conditions for VDAC were identified and allowed further characterization of VDAC and its interactions by NMR and other methods. Obtained through various means, evidence of a concentration dependent self-association of VDAC is also presented. Chemical cross-linking, analytical size exclusion chromatography, and NMR spectroscopic studies strongly support an equilibrium model for LDAO-purified VDAC between monomer and trimer.
(cont.) Methods that were necessary to carry out NMR structural studies of VDAC and results from those studies are described. In addition to various methods previously developed for solution NMR spectroscopy of very large proteins, extensive labeling approaches and unconventional experimental NMR methods were necessary to obtain a high level of chemical shift assignment for micelle-bound VDAC. Chemical shift assignment has allowed the preliminary characterization of ATP and Bcl-xL binding to VDAC. Binding of Bcl-xL, a central regulator of apoptosis, to VDAC is demonstrated here. Using NMR spectroscopy, the VDAC-binding region of Bcl-xL has been mapped to a putative helical hairpin motif, which also mediates insertion into membranes. The stoichiometry of the VDAC/Bcl-xL complex is shown to be a heterotrimer of two VDAC monomers and one Bcl-xL. The demonstration of VDAC/Bcl-xL complex formation supports the concept that components of apoptosis and metabolism are integrally connected, and that interplay between the two processes is required for regulation of cell survival and cell death.
Ph.D.