Dissertations / Theses on the topic 'Substrate-binding proteins'
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Hendry, Garth S. "Dependence of substrate-water binding on protein and inorganic cofactors of photosystem II /." View thesis entry in Australian Digital Theses Program, 2002. http://thesis.anu.edu.au/public/adt-ANU20041124.140348/index.html.
Full textFesser, Stephanie Marion. "Contribution of RNA binding proteins to substrate specificity in small RNA biogenesis." Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-173105.
Full textGarza, John Anthony. "Structural and ligand-binding properties of a dual substrate specific enzymes from schizosaccharomyces pombe a dissertation /." San Antonio : UTHSC, 2009. http://learningobjects.library.uthscsa.edu/cdm4/item_viewer.php?CISOROOT=/theses&CISOPTR=45&CISOBOX=1&REC=17.
Full textSarma, Ranjana. "Investigations of nucleotide-dependent electron transfer and substrate binding in nitrogen fixation and chlorophyll biosynthesis." Thesis, Montana State University, 2009. http://etd.lib.montana.edu/etd/2009/sarma/SarmaR1209.pdf.
Full textJaya, Nomalie Naomi. "SUBSTRATE BINDING SITE FLEXIBILITY OF SMALL HEAT SHOCK PROTEINS AND FACTORS CONTRIBUTING TO EFFICIENT CHAPERONE ACTIVITY." Diss., The University of Arizona, 2009. http://hdl.handle.net/10150/193550.
Full textHendry, Garth S., and Garth Hendry@baldwins com. "Dependence of substrate-water binding on protein and inorganic cofactors of photosystem II." The Australian National University. Research School of Biological Sciences, 2002. http://thesis.anu.edu.au./public/adt-ANU20041124.140348.
Full textFesser, Stephanie Marion [Verfasser], and Klaus [Akademischer Betreuer] Förstemann. "Contribution of RNA binding proteins to substrate specificity in small RNA biogenesis / Stephanie Marion Fesser. Betreuer: Klaus Förstemann." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2013. http://d-nb.info/1055907793/34.
Full textYuan, Ming. "Antiphagocytosis by Yersinia pseudotuberculosis : role of the YopH target proteins." Doctoral thesis, Umeå : Umeå University, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-957.
Full textWisniewska, Magdalena. "Biochemical studies on IGF and IGF-binding proteins interactions & structural investigations on the SH3 domain of Crk-associated tyrosine kinase substrate p130cas (CAS)." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=978198549.
Full textEscobedo, Pascual Albert. "Structural Insights into Substrate Binding and Regulation of E3 Ubiquitin Ligases in the Nedd4 Family using NMR Spectroscopy." Doctoral thesis, Universitat de Barcelona, 2014. http://hdl.handle.net/10803/284605.
Full textNedd4L és una E3 ubiquitín lligasa responsable de la regulació de la vida mitja del canal de sodi ß-ENaC i de Smad2/3, proteïnes mediadores de la ruta de senyalització activada per citocines TGF-ß. Defectes en la seva funció han estat relacionats amb la hipertensió hereditària (Síndrome de Liddle), i podrien ser rellevants en determinats tipus de càncer i metàstasi. CDK8/9 i GSK3-ß són dues quinases que regulen l’estat de fosforilació de les Smads, habilitant-les per dur a terme llur funció en cooperació amb factors de transcripció al mateix temps que les marquen per ser reconegudes per ubiquitín lligases. Amb l’objectiu d’identificar els residus i els patrons de fosforilació rellevants hem preparat un set de fosfopèptids que corresponen a les seqüències de Smad1/3. Nedd4L presenta una arquitectura multi-domini C2-WW-HECT. Diverses lligases de la família de Nedd4 existeixen en una conformació latent en què contactes inter-domini oclouen el lloc catalític en el domini HECT, involucrant bé el domini C2 (Smurf1/2, WWP2, Nedd4, Nedd4L) o la zona central amb els dominis WW (Itch). Certs esdeveniments cel•lulars desplacen aquests contactes, induint la transició a la conformació activa. L’increment dels nivells intracel•lulars de Ca2+ activa Nedd4L. La hidròlisi del fosfolípid de membrana PIP2 allibera l’IP3 provocant aquest increment. El domini C2 de Nedd4L interacciona tant amb el Ca2+ com amb l’IP3. Utilitzant l’RMN hem descrit els contactes HECT-C2 en la conformació latent i hem observat que el Ca2+ s’uneix al domini C2 amb alta afinitat utilitzant el mateix lloc d’unió, a més d’afavorir la interacció amb l’IP3. Així, hem aportat el fonament estructural per a l’activació i relocalització a la membrana cel•lular de Nedd4L. El domini HECT presenta un lloc PY altament conservat (HECT-PY). Els motius PY són reconeguts pels dominis WW. Proposem que el reconeixement del motiu HECT-PY per part d’un dels dominis WW de Nedd4L estigui implicat en l’auto-ubiquitinació. Hem observat que només quan el plegament del domini HECT està compromès, el lloc PY és accessible. Presentem l’estructura per RMN del complex WW3-HECT-PY. El motiu està protegit en molècules funcionals de Nedd4L, capaces de reconèixer-lo en molècules danyades i ubiquitinar-les.
Dabrowski, Christian. "Mutagenesis of the substrate binding site of protein disulfide isomerase." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66879.
Full textLa protéine disulfure isomérase (PDI) est le membre le mieux connu et caractérisé de la nombreuse famille de PDI qui se trouve dans le réticulum endoplasmique. PDI joue un rôle important dans le repliement des chaînes protéiques. Elle est composée de quatre domaines désignés a-b-b'-a' de type thiorédoxine. Des études récentes ont identifié une surface hydrophobe dans le domaine b' comme étant le lieu principal d'interaction avec les substrats déroulés de la PDI. Ici, les résidus hydrophobes principaux du domaine b' ont été mutés et testés pour leur interaction avec un peptide de quatorze résidus nommé mastoparan. La plupart des mutants ont eu un impact important sur l'affinité de la PDI pour son substrat. Dans des expériences contraires où le peptide mastoparan a été muté, des titrations par RMN ont révélé l'orientation du peptide sur la surface d'interaction du domaine b'. Finalement, les domaines catalytiques a et a' ont été individuellement testés par RMN pour leur affinité envers l'ARNase A déroulée. Les deux domaines n'ont montré aucune interaction avec le substrat déroulé.
Farah, Sahar. "Identification of Rho-associated protein kinaseà as an insulin receptor substrate-1 binding protein." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ28422.pdf.
Full textMorris, Benjamin L. "Understanding and targeting the C-terminal Binding Protein (CtBP) substrate-binding domain for cancer therapeutic development." VCU Scholars Compass, 2016. http://scholarscompass.vcu.edu/etd/4434.
Full textFarah, Sahar. "Identification of Rho-associated protein kinase-alpha as an insulin receptor substrate-1 binding protein." Thesis, University of Ottawa (Canada), 1998. http://hdl.handle.net/10393/4152.
Full textChen, Ce-Belle. "The role of mannose-binding protein-associated serine proteases in complement activation : interactions with mannose-binding protein and mode of substrate recognition." Thesis, University of Oxford, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400560.
Full textFischer, Marcus. "Structural biophysics of ligand, fragment and water interactions with substrate binding protein SiaP." Thesis, University of York, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.542843.
Full textKnight, James D. R. "The Structural and Functional Identity of the Protein Kinase Superfamily." Thesis, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/20232.
Full textCourt, Naomi Wynne. "The subcellular localisation, tissue expression, substrate specificity and binding partners of stress-activated protein kinase-3." University of Western Australia. School of Biomedical and Chemical Sciences, 2004. http://theses.library.uwa.edu.au/adt-WU2004.0084.
Full textWagner, Judith Nastjenka. "The HSP100 protein ClpA: Significance of the N-terminal domain in substrate recognition and binding and characterization of the novel substrate RepE." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:25-opus-60188.
Full textWalter, Julia [Verfasser]. "The Autopalmitoylated Vesicular Transport Protein Bet3 : Biochemical and Fluorescence-based Characterization of Membrane and Substrate Binding / Julia Walter." Berlin : Freie Universität Berlin, 2018. http://d-nb.info/1155761081/34.
Full textWang, Fen. "In silico and in vitro determination of substrate specificity for Breast Cancer Resistance Protein (BCRP) transporter at the blood-brain barrier." Thesis, Uppsala universitet, Institutionen för farmaci, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-444527.
Full textPetrovic, Dusan [Verfasser], Birgit [Akademischer Betreuer] Strodel, Christel M. [Gutachter] Marian, and Johannes [Gutachter] Kästner. "Computational Enzyme Evolution and Design: Studies of Protein Dynamics and Substrate Binding / Dusan Petrovic ; Gutachter: Christel M. Marian, Johannes Kästner ; Betreuer: Birgit Strodel." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2018. http://d-nb.info/1163108065/34.
Full textSukumar, Preethi. "Molecular dissection of substrate and inhibitor binding to the D-galactose-H⁺ symport protein (GalP) from Escherichia coli - the bacterial homologue of GLUT1." Thesis, University of Leeds, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.713697.
Full textJanke, Kirsten [Verfasser], Eric [Akademischer Betreuer] Metzen, and Verena [Akademischer Betreuer] Jendrossek. "Characterisation of apoptosis-stimulating p53 binding protein 2 (ASPP2) as a new substrate for asparaginyl hydroxylation / Kirsten Janke. Gutachter: Verena Jendrossek. Betreuer: Eric Metzen." Duisburg, 2013. http://d-nb.info/1042373507/34.
Full textSanford, Brianne. "Role of Coupled Dynamics and a Strictly Conserved Lysine Residue in the Function of Bacterial Prolyl-tRNA Synthetase and Substrate Binding by a Related trans-Editing Enzyme ProXp-ala." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1397645941.
Full textSubramaniam, Srisunder. "Studies of conformational changes and dynamics accompanying substrate recognition, allostery and catalysis in bacteriophage lambda integrase." The Ohio State University, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=osu1111655332.
Full textChakrabarti, Kalyan Sundar. "Solution Structural Studies And Substrate Binding Properties Of The Amino-Terminal Domain Of E.coli Pantothenate Synthetase." Thesis, 2008. http://hdl.handle.net/2005/1103.
Full textHendry, Garth S. "Dependence of substrate-water binding on protein and inorganic cofactors of photosystem II." Phd thesis, 2002. http://hdl.handle.net/1885/47151.
Full textWisniewska, Magdalena [Verfasser]. "Biochemical studies on IGF and IGF-binding proteins interactions & structural investigations on the SH3 domain of Crk-associated tyrosine kinase substrate p130cas (CAS) / Magdalena Wisniewska." 2005. http://d-nb.info/978198549/34.
Full textMühlhausen, Helene. "Untersuchungen zur molekularen Ursache der Multiplen Sulfatase-Defizienz: Reinigung, Funktions- und Strukturanalyse von varianten Proteinen des Formylglycin-generierenden Enzyms." Doctoral thesis, 2014. http://hdl.handle.net/11858/00-1735-0000-0023-9953-2.
Full textPinto, Bárbara Palma de Abreu Caldeira. "Studies on the function and substrate permeation in ABC transporters by biomolecular simulations." Doctoral thesis, 2021. http://hdl.handle.net/10362/121941.
Full textFisher, Loren Tichauer. "Role of a topologically conserved Isoleucine in the structure and function of Glutathione Transferases." Thesis, 2006. http://hdl.handle.net/10539/1726.
Full textProteins in the glutathione transferase family share a common fold. The close packing of secondary structures in the thioredoxin fold in domain 1 forms a compact hydrophobic core. This fold has a bababba topology and most proteins/domains with this fold have a topologically conserved isoleucine residue at the N-terminus of a-helix 3. Class Alpha glutathione transferases are one of 12 classes within the glutathione transferase family. To investigate the role of the conserved isoleucine residue in the structure, function and stability of glutathione transferases, homodimeric human glutathione transferase A1-1 (hGST A1-1) was used as a representative of the GST family. Ile71 was replaced with valine and the properties of I71V hGST A1-1 were compared with those of wildtype hGST A1-1. The spectral properties monitored using far-UV CD and tryptophan fluorescence indicated little change in secondary or tertiary structure confirming the absence of any gross structural changes in hGST A1-1 due to the incorporation of the mutation. Both wildtype and mutant dimeric proteins were determined to have a monomeric molecular mass of 26 kDa. The specific activity of I71V hGST A1-1 (130 mmol/min/mg) was three times that of wildtype hGST A1-1 (48 mmol/min/mg). I71V hGST A1-1 showed increased kinetic parameters compared to wildtype with a 10-fold increase in kcat/Km for CDNB. The increase in Km of I71V hGST A1-1 suggests the mutation had a negative effect on substrate binding. The DDG for transition state stabilisation was –5.82 kJ/mol which suggest the I71V mutation helps stabilise the transition state of the SNAR reaction involving the conjugation of reduced glutathione (GSH) to 1-chloro-2,4-dinitrobenzene (CDNB). A 2-fold increase in the IC50 value for I71V hGST A1-1 (11.3 mM) compared to wildtype (5.4 mM) suggests that the most noticeable change due to the mutation occurs at the H-site of the active site. Conformational stability studies were performed to determine the contribution of Ile71 to protein stability. The non-superimposability of I71V hGST A1-1 unfolding curves and the decreased m-value suggest the formation of an intermediate state. The conformational stability of I71V hGST A1-1 (16.5 kcal/mol) was reduced when compared to that of the wildtype (23 kcal/mol). ITC was used to dissect the binding energetics of Shexylglutathione to wildtype and I71V hGSTA1-1. The ligand binds 5-fold more tightly to wildtype hGST A1-1 (0.07 mM) than I71V hGST A1-1 (0.37 mM). The I71V mutant displays a larger negative DCp than wildtype hGST A1-1 (DDCp = -0.41 kJ/mol/K). This indicates that a larger solvent-exposed hydrophobic surface area is buried for I71V hGST A1-1 than for wildtype hGST A1-1 upon the binding of S-hexylglutathione. Overall the results suggest that Ile71 conservation is for the stability of the protein as well as playing a pivotal indirect role in catalysis and substrate binding.
Wagner, Judith Nastjenka [Verfasser]. "The HSP100 protein ClpA : significance of the N-terminal domain in substrate recognition and binding and characterization of the novel substrate RepE / vorgelegt von Judith Nastjenka Wagner." 2008. http://d-nb.info/991293142/34.
Full textBarker, Megan. "Structural Investigation of Processing α-Glucosidase I from Saccharomyces cerevisiae." Thesis, 2010. http://hdl.handle.net/1807/32660.
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