Дисертації з теми "Structure and Dynamics of Peptides by NMR Spectroscopy"
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Tengel, Tobias. "Studies of protein structure, dynamics and protein-ligand interactions using NMR spectroscopy." Doctoral thesis, Umeå : Univ, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1472.
Повний текст джерелаAmero, Carlos D. "Protein Function Study by NMR Spectroscopy." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1205431343.
Повний текст джерелаDebelouchina, Galia Tzvetanova. "Amyloid fibril structure of peptides and proteins by magic angle spinning NMR spectroscopy and dynamic nuclear polarization." Thesis, Massachusetts Institute of Technology, 2011. http://hdl.handle.net/1721.1/68485.
Повний текст джерелаVita. Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references.
Amyloid fibrils are insoluble, non-crystalline protein filaments associated with a number of diseases such as Alzheimer's and Type Il diabetes. They can have a functional role in different organisms and many proteins and peptides have been found to form amyloid fibrils in vitro. We have used magic angle spinning (MAS) NMR spectroscopy to investigate the structure of two amyloid fibril systems - an 11- residue segment from the disease-related protein transthyretin (TTR); and P2- microglobulin (32m), a 99-residue protein associated with dialysis-related amyloidosis. The TTR(105-115) case exemplifies our efforts to characterize the hierarchy of structures present in the fibril form, including the organization of the Pstrands into P-sheets (tertiary structure), the P-sheet interface that defines each protofilament (quaternary structure), and the protofilament-to-protofilament contacts that lead to the formation of the complete fibril. Our efforts were guided by information obtained from other methods such as cryo-electron microscopy and atomic force microscopy, and resulted in the very first atomic resolution structure of a complete amyloid fibril. We have extended the methods used in the TTR(105-115) structure determination procedure to the fibrils formed by 2m, a process complicated not only by the much larger size of the protein involved but also by the high degree of dynamics exhibited in these fibrils. Nevertheless, we were able to characterize the secondary structure of the protein in the fibril form, and the tertiary and quaternary interactions within the fibrils. In addition, we have compared at the molecular level @2m fibrils formed under different conditions, in an effort to characterize the origins of fibril polymorphism for this protein sequence. Our work on amyloid fibrils has also benefited extensively from the development of dynamic nuclear polarization, a method used to enhance the sensitivity of MAS NMR experiments, leading to unprecedented gains in signal-to-noise ratios and acquisition times.
by Galia Tzvetanova Debelouchina.
Ph.D.
Unnikrishnan, Aparna. "INVESTIGATION OF PROTEIN STRUCTURE AND DYNAMICS BY NMR SPECTROSCOPY." The Ohio State University, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1595418229203869.
Повний текст джерелаThurgood, Andrew G. P. "NMR studies of the structure and dynamics of proteins and peptides." Thesis, University of East Anglia, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253623.
Повний текст джерелаRönnols, Jerk. "Structure, dynamics and reactivity of carbohydrates : NMR spectroscopic studies." Doctoral thesis, Stockholms universitet, Institutionen för organisk kemi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-92408.
Повний текст джерелаAt the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 4: Submitted. Paper 5: Manuscript.
Conroy, Daniel William. "Structural Studies of Biomolecules by Dynamic Nuclear Polarization Solid-State NMR Spectroscopy." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1555428362333615.
Повний текст джерелаNagapudi, Karthik. "Solid-state NMR investigation of structure and dynamics of polyrotaxanes." Thesis, Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/8638.
Повний текст джерелаTomaszewski, John William. "Structure and dynamics of small proteins by NMR /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/11541.
Повний текст джерелаBirk, Olsen Helle. "Investigations of structure and dynamics of insulin mutants using NMR spectroscopy /." Roskilde : Department of Life Sciences and Chemistry, Roskilde University, 1996. http://hdl.handle.net/1800/464.
Повний текст джерелаThirumoorthy, Ramanan. "NMR studies of structure and dynamics of novel peptide-based melanocortin receptor antagonists." [Gainesville, Fla.] : University of Florida, 2002. http://purl.fcla.edu/fcla/etd/UFE1001186.
Повний текст джерелаDrew, Daniel L. Jr. "Investigating the Structure and Dynamic Properties of Bacteriophage S21 Pinholin Using Solid-State Nuclear Magnetic Resonance and Electron Paramagnetic Resonance Spectroscopy." Miami University / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=miami1610187893016095.
Повний текст джерелаDallmann, André. "Structure and dynamics of fluorophore-labelled DNA helices probed by NMR-spectroscopy." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2010. http://dx.doi.org/10.18452/16065.
Повний текст джерелаStructural and dynamic perturbations in DNA upon incorporation of either fluorophore, 2-Aminopurine (2AP) or 2-Hydroxy-7-nitrofluorene (HNF), are characterized by NMR spectroscopy. For this purpose the NMR solution structures of the modified DNA duplexes with the sequence 5’-GCTGCAXACGTCG-3’ are solved. For X=2AP (13mer2AP) the partner base in the complementary strand is T, while for X=HNF (13merHNF) an abasic site is introduced to avoid steric strain. By comparing results on 13mer2AP with the corresponding unmodified DNA duplex (13merRef, X=A), any perturbation can be unambiguously assigned to 2AP incorporation. For the NMR solution structure of 13merRef and 13mer2AP small but significant changes in helical parameters are found throughout the helix. Imino proton exchange measurements reveal an extended, distributed effect of 2AP incorporation on the lifetimes of the central seven base pair. However, the reduced base pair lifetime of 2AP:T cannot fully account for the rapid water exchange observed with saturation transfer experiments in the absence of base catalyst. This indicates enhanced intrinsic catalysis. As a possible catalytic site the T O4 atom opposite 2AP is discussed, which is easily accessible through the major groove and lacks a hydrogen bonding partner within the base pair. The overall NMR solution structure is found to be B-DNA. However the NOE cross-peaks involving the HNF residue can only be accounted for by two different orientations of the HNF inside the DNA helical stack. Their population ratio is estimated to be 1:1. Dynamical perturbation is indicated by the increased linewidth and strong upfield shift of the T residue to the 5’-side of the abasic site.
Wang, Tuo Ph D. Massachusetts Institute of Technology. "Structure and dynamics of plant cell walls and membrane peptides from solid-state NMR." Thesis, Massachusetts Institute of Technology, 2016. http://hdl.handle.net/1721.1/103710.
Повний текст джерелаCataloged from PDF version of thesis.
Includes bibliographical references.
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique to study the structure, dynamics and interactions of bio-macromolecules. This thesis mainly focuses on the characterization of the architecture and loosening of primary plant cell walls and the interactions between membrane and peptides. Plant cell wall is a complex system mainly comprising three types of insoluble polysaccharides: cellulose, hemicellulose and pectin. The spatial arrangement of these macromolecules has been largely elusive due to the lack of high-resolution and sitespecific characterization techniques. Here, we introduce SSNMR to investigate the interactions of macromolecules in ¹³C-labeled plant primary cell walls with minimal treatment. Our multidimensional ¹³C spectra show intense cellulose-pectin correlations, suggesting subnanometer contacts between these polymers. The cellulose-pectin interaction is found to be an inherent feature of primary cell walls because it is independent of the hydration history and is caused by site-specific interactions instead of molecular crowding. By measuring water to polysaccharide spin diffusion in intact and sequentially digested walls, we are able to examine the three-dimensional structure of cell walls. Our results suggest a single network model, where cellulose microfibrils make physical contacts with both pectin and hemicellulose. We also investigated how this network was unlocked by expansin, a wall-loosening protein. Using differential isotopic labeling and dynamic nuclear polarization, we determined the binding sites of 0.2 mg expansin in cell walls. Cellulose microfibrils with entrapped hemicellulose were found to be the targets of expansins, thus shedding light on the mechanisms of wall elongation and plant growth. These results have deepened our understanding of plant cell walls, a smart material with both high mechanical strength and extensibility. In addition, we also developed new approaches to investigate the interactions between membranes and peptides. By measuring heteronuclear correlation spectra and proton relaxation times, we determined the localization of the Influenza M2 peptide in distinctly curved membrane domains. Using a rigid-solid heteronuclear correlation experiment, we were able to determine the depth of insertion of dynamically invisible peptides in gel-phase membranes. These studies provide new strategies to study the functionally relevant membrane-curvature induction by proteins and the partitioning and insertion of proteins into lipid membranes.
by Tuo Wang.
Ph. D.
Rapp, Almut. "Structure and dynamics of supramolecular assemblies studied by advanced solid-state NMR spectroscopy." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969937962.
Повний текст джерелаXu, Xiaolin, and Xiaolin Xu. "Theory and Applications of Solid-State NMR Spectroscopy to Biomembrane Structure and Dynamics." Diss., The University of Arizona, 2017. http://hdl.handle.net/10150/626369.
Повний текст джерелаLandström, Jens. "Structure, dynamics and interactions of biomolecules : investigations by NMR spectroscopy and computational methods /." Stockholm : Department of Organic Chemistry, Stockholm University, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-30120.
Повний текст джерелаAt the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Submitted. Paper 4: Submitted. Paper 5: In progress. Paper 6: In progress. Paper 7: Manuscript. Härtill 7 uppsatser.
Philippopoulos, Marios. "Comparative studies of protein structure and dynamics by molecular dynamics simulation, NMR spectroscopy and x-ray crystallography." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq41038.pdf.
Повний текст джерелаFlodell, Sara. "Structure and Dynamics of the Hepatitis B Virus Encapsidation Signal Revealed by NMR Spectroscopy." Doctoral thesis, Umeå : Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-316.
Повний текст джерелаBrodsky, Alexander S. (Alexander Simon) 1970. "Structure and dynamics of the HIV-2 TAR RNA-argininamide complex by NMR spectroscopy." Thesis, Massachusetts Institute of Technology, 1998. http://hdl.handle.net/1721.1/49982.
Повний текст джерелаZhu, Leiming. "A study of spin dynamics and molecular structure of nucleic acids by NMR /." Thesis, Connect to this title online; UW restricted, 1994. http://hdl.handle.net/1773/11543.
Повний текст джерелаYing, Jinfa. "Studies of biologically active peptides by NMR and molecular dynamics simulations: From structure and dynamics to design and synthesis." Diss., The University of Arizona, 2004. http://hdl.handle.net/10150/280667.
Повний текст джерелаGuan, Xiao, and 关晓. "NMR approaches to protein conformation and backbone dynamics: studies on hyperthermophilicacylphosphatase and neuropeptide secretoneurin." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B44079230.
Повний текст джерелаWagstaff, Jane Louise. "Structure, dynamics and interaction studies of integrin avb6 specific peptides using nuclear magnetic resonance spectroscopy." Thesis, University of Kent, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.544092.
Повний текст джерелаLi, Xing. "Structure and dynamics of alamethicin dimers by high-resolution proton and nitrogen-15 NMR spectroscopy." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0026/MQ51741.pdf.
Повний текст джерелаLi, Xing. "Structure and dynamics of alamethicin dimers by high-resolution proton and nitrogen-15 NMR spectroscopy." Ottawa : National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.nlc-bnc.ca/obj/s4/f2/dsk1/tape2/PQDD%5F0026/MQ51741.pdf.
Повний текст джерелаIwakawa, Naoto. "Dynamic Structural Changes of Proteins Revealed by NMR Spectroscopy Under Physicochemical Perturbations." Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263679.
Повний текст джерелаJohn, Michael. "Structure and exchange dynamics of the apical domains of the thermosome and human saposins by NMR spectroscopy." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972320008.
Повний текст джерелаAbu-Baker, Shadi. "Solid-State NMR Spectroscopic Studies on Phospholamban and Saposin C Proteins in Phospholipid Membranes." Miami University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=miami1185851259.
Повний текст джерелаGhimire, Harishchandra. "Structure, Dynamics, and Distance Measurements in Membrane Proteins and Peptides using EPR Spectroscopic Techniques." Miami University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=miami1291739688.
Повний текст джерелаHudson, Frederick Michael Lewis. "NMR characterization guides the design of beta hairpins and sheets while providing insights into folding cooperativity and dynamics /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/8639.
Повний текст джерелаGao, Xinfeng. "Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation /." free to MU campus, to others for purchase, 2004. http://wwwlib.umi.com/cr/mo/fullcit?p3137700.
Повний текст джерелаWhittaker, Sara Britt-Marie. "An investigation into the structure and dynamics of the DNase domain of colicin E9 by heteronuclear NMR spectroscopy." Thesis, University of East Anglia, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266728.
Повний текст джерелаGranata, Daniele. "Characterizing Structure and Free Energy Landscape of Proteins by NMR-guided Metadynamics." Doctoral thesis, SISSA, 2013. http://hdl.handle.net/20.500.11767/4824.
Повний текст джерелаSahakyan, Aleksandr B. "Extending the boundaries of the usage of NMR chemical shifts in deciphering biomolecular structure and dynamics." Thesis, University of Cambridge, 2012. https://www.repository.cam.ac.uk/handle/1810/243642.
Повний текст джерелаShannon, Matthew D. "High Resolution Structural and Dynamic Studies of Biomacromolecular Assemblies using Solid-State NMR Spectroscopy." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1534321838601796.
Повний текст джерелаKim, Gunwoo. "Understanding local structure and dynamics of the proton-conducting solid electrolytes CsH₂PO₄ and CsH(PO₃H) by solid-state NMR spectroscopy." Thesis, University of Cambridge, 2014. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708211.
Повний текст джерелаIordanov, Iordan. "Structure and dynamics of the outer membrane protein A from Klebsiella pneumoniae : a joint NMR–SMFS–proteolysis and MS approach." Toulouse 3, 2012. http://thesesups.ups-tlse.fr/1602/.
Повний текст джерелаKpOmpA is a two-domain membrane protein from Klebsiella pneumoniae belonging to the outer membrane protein A (OmpA) family. It is composed of a transmembrane ß-barrel with 8 ß-strands and a C-terminal, soluble periplasmic domain. The transmembrane domain presents a significant homology with E. Coli OmpA whose three dimensional structure has been determined by X-ray crystallography and by NMR. The E. Coli homologue can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages. It is assumed that most of these functions involve the four protein loops that emanate from the protein to the exterior of the cell. The difference between KpOmpA and E. Coli OmpA is mostly concentrated in these extracellular loops which are larger in the case of KpOmpA. KpOmpA was shown to activate macrophages and dendritic cells through the TLR2 dependent pathway, and these larger loops are supposed to play a specific role in the interactions with the immune system. Thus the structure and dynamics of these loops is of prime functional significance. The currently available information in this regard, including the NMR structure determined in the IPBS NMR group in 2009, have been obtained so far with recombinant protein samples purified and refolded in detergent micelles. In the present work we first established a reconstitution protocol that allowed the incorporation of the membrane protein in the more native environment of the lipid bilayer and characterised our samples by electron microscopy. SMFS experiments were used to probe the reconstituted KpOmpA unfolding-refolding pathways, exploring the folding mechanisms for ß-barrel proteins and suggesting a novel role for OmpA in the bacterial membrane (in collaboration with the group of D. Müller, ETH Zürich). The C-terminal periplasmic domain of KpOmpA was expressed and purified as a separate product and the feasibility of its structure elucidation by NMR was demonstrated by obtaining a high quality HSQC spectrum. The dynamic behaviour of the extracellular portion of the KpOmpA membrane domain reconstituted in liposomes has been investigated by solid state MAS NMR relaxation experiments. We confirmed that the previously observed gradient of dynamic along the molecule axis is an intrinsic property of the protein. Limited proteolysis and MALDI-TOF experiments were coupled with the NMR information in order to assess more precisely the different mobility levels in the loops. Evolutional preservation of the different loops regions is related to their observed flexibility, pointing towards immunologically important, variable, dynamic and accessible loops sections
Lignell, Martin. "Structural Transitions in Helical Peptides : The Influence of Water – Implications for Molecular Recognition and Protein Folding." Doctoral thesis, Uppsala universitet, Kemisk fysik, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-109396.
Повний текст джерелаHanni, M. (Matti). "Static and dynamic NMR properties of gas-phase xenon." Doctoral thesis, University of Oulu, 2011. http://urn.fi/urn:isbn:9789514294570.
Повний текст джерелаJean-François, Frantz. "Vers un nouveau mode d’action de peptides antimicrobiens structurés en feuillets ß : formation de domaines membranaires par la cateslytine." Thesis, Bordeaux 1, 2008. http://www.theses.fr/2008BOR13638/document.
Повний текст джерелаThe antimicrobial peptide Cateslytin (bCGA RSMRLSFRARGYGFR ) is a five positively charged arginin rich peptide known to inhibit the release of catecholamine in chromaffin granules. Although biological data showed that it is able to inhibit the growth of several microorganisms such as bacteria, yeast and Plasmodium falciparum parasite involved in malaria, the mechanism of action has not been yet studied. In order to better understand both targeting and selectivity of this peptide towards microorganisms, model membranes of variable compositions have been chosen to respectively mimic microorganisms or mammalian membranes. Structural studies have been performed using polarised ATR-FTIR, circular dichroïsm and high resolution NMR Membrane dynamics has been followed using deuterium labelled lipids and solid state NMR Patch clamp experiments were also performed on lipid vesicles to measure channe conductivity. All-atom molecular dynamics on hydrated peptide-lipid membrane systems was also used to assess the interaction from the atomic level. Main results from this interdisciplinary approach are three-fold. i) Electric current passages through membranes demonstrate permeation akin to pore formation. ii) Peptide-induced formation of rigid domains mainly made of negatively charged lipids is found. iii) Peptide antiparallel ß-sheets are observed preferentially with negatively charged lipids mimicking microorganism membranes. The general picture leads to the proposal that membrane destabilization/permeation is promoted by rigid domains stabilised by peptide ß-sheets
Asami, Sam [Verfasser], Bernd [Akademischer Betreuer] Reif, Andreas [Akademischer Betreuer] Möglich, and Hartmut [Akademischer Betreuer] Oschkinat. "Method development for biomolecular solid-state NMR spectroscopy : accessing structure and dynamics of biomolecules in the solid-state / Sam Asami. Gutachter: Bernd Reif ; Andreas Möglich ; Hartmut Oschkinat." Berlin : Humboldt Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://d-nb.info/1060425262/34.
Повний текст джерелаAsami, Sam [Verfasser], Bernd Akademischer Betreuer] Reif, Andreas [Akademischer Betreuer] Möglich, and Hartmut [Akademischer Betreuer] [Oschkinat. "Method development for biomolecular solid-state NMR spectroscopy : accessing structure and dynamics of biomolecules in the solid-state / Sam Asami. Gutachter: Bernd Reif ; Andreas Möglich ; Hartmut Oschkinat." Berlin : Humboldt Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://nbn-resolving.de/urn:nbn:de:kobv:11-100220957.
Повний текст джерелаMigliore, Mattia. "Recherche par modélisaion moléculaire de signatures RMN et DC caractéristiques pour les coudes β et y dans les peptides bioactifs. Characterization of β-turns by electronic circular dichroism spectroscopy : a coupled molecular dynamics and time-dependent density functional theory computational study". Thesis, Normandie, 2020. http://www.theses.fr/2020NORMR001.
Повний текст джерелаThe aim of this work is to identify NMR and CD characteristic patterns for β- and γ-turns in bioactive peptides by molecular modelling. With helices, β- and γ-turns constitute favoured recognition motifs in bioactive peptides by their targets. Even though several classes of turns with different geometries exist in polypeptide structures (2 γ-turn types and 12 β-turn types), few experimental tools are available for their characterization. Thus, only 4 types of β-turns (I, I’, II et II’) have been, at present, described by NMR and there are no reliable reference CD spectra for turns. In order to extend the NMR data for all β- and γ-turn types, we analyzed NMR structural parameters (inter-hydrogen distances and ᶾJʜɴ-ʜꭤ coupling constants) in a representative peptide model dataset extracted from the PDB. The inter-hydrogen distance analysis allowed to identify specific NMR patterns for the two γ-turn types and for four β-turn types (IV₁, IV₂,, VIb and VIII). ᶾJʜɴ-ʜꭤ coupling constant may be used to confirm the identification and to remove ambiguities. Then, we simulated the reference CD spectra of model peptides adopting type I, I’, II and II’ β-turn conformations by combining molecular dynamic simulations and TDDFT computations. These computations allowed to determine two families of specific CD spectra : types I/II’, on one side and types I’/II, on the other. All these results indicate that the turns do not present the same patterns in both techniques. The combination of NMR and CD could therefore allow a better identification of the nature and the different types of turns
Weinhaeupl, Katharina. "Etudes de structure, interactions et dynamique dans des complexes de protéines "chaperone" à l'échelle atomique par spectroscopie RMN." Thesis, Université Grenoble Alpes (ComUE), 2018. http://www.theses.fr/2018GREAV002.
Повний текст джерелаThe diverse group of molecular chaperones is dedicated to accompany, fold and protect other proteins until they reach their final conformation and loca- tion inside the cell. To this end, molecular chaperones need to be specialized in performing specific tasks, like folding, transport or disaggregation, and versatile in their recognition pattern to engage many di erent client pro- teins. Moreover, molecular chaperones need to be able to interact with each other and with other components of the protein quality control system in a complex network. Interactions between the di erent partners in this network and between the substrate and the chaperone are often dynamic processes, which are especially di cult to study using standard structural biology tech- niques. Consequently, structural data on chaperone/substrate complexes are sparse, and the mechanisms of chaperone action are poorly understood. In this thesis I present investigations of the structure, dynamics and substrate- interactions of two molecular chaperones, using various biophysical and in vivo methods.In the first part I show that the mitochondrial membrane protein chap- erone TIM910 binds its substrates in a highly dynamic manner. Not only is the TIM910 complex in constant exchange between monomeric and hex- americ species, but also the bound substrate samples multiple conformations on a millisecond timescale. Based on nuclear magnetic resonance (NMR), small-angle X-ray scattering (SAXS), analytical ultracentrifugation (AUC) and in vivo mutational experiments I propose a structural model of the chap- erone/membrane protein interaction. TIM910 binds its substrates in a hy- drophobic pocket on the exterior of the chaperone in a modular fashion, where the number of TIM910 complexes bound depends on the length of the substrate.In the second part I studied the behavior of the N-terminal receptor do- main of the ClpC1 unfoldase from M.tuberculosis in the presence of di erent antibiotics and ligands. The N-terminal domain of ClpC1 is the binding site for various new antibiotics against M.tuberculosis. The antibiotic cyclomarin completely abolishes dynamics induced by the ligand arginine-phosphate. We propose that this suppression of dynamics is the underlying principle for the mechanism of action of this antibiotic.In both cases X-ray structures of the apo or antibiotic bound form were available, but not su cient to explain the mechanism of action. The X- ray structure of TIM910 provided no evidence on where or how substrates are bound. Likewise, X-ray structures of the apo and cyclomarin-bound N-terminal domain of ClpC1 show only minor di erences in structure.Both examples show that static structural data is often not enough to explain how a molecular system works, and only the combination of di er- ent techniques, including newly developed methods enable the atomic-level understanding of chaperone/substrate complexes
Li, Xuesong. "Synthesis and physical properties of helical nanosized quinoline-based foldamers : structure, dynamics and photoinduced electron transport." Thesis, Bordeaux, 2016. http://www.theses.fr/2016BORD0013/document.
Повний текст джерелаHerein, synthesis, characterization and application (photoinduced electron transport) of nanosized quinoline-based foldamers have been explored. With double segment strategy, a variety of helical nanosized foldamers (up to 96 quinoline units) were successfully prepared based on 8-aminoquinoline-2-carboxylic acid monomer.The dynamic properties in gas phase and solution were investigated. Ion mobility mass spectrometry afforded access to the conformation state of foldamers ingas phase; DOSY and fluorescence anisotropy assessed the diffusion (translational and rotational, respectively) of foldamers in solution. All of these techniques revealed that quinoline-based foldamers are rigid and that helical conformation is conserved. Photoinduced electron transport through nanosized foldamer was also studied and the mechanism and the transport ratios were revealed
Andronesi, Ovidiu-Cristian. "Solid-state NMR of (membrane) protein complexes novel methods and applications /." Doctoral thesis, [S.l.] : [s.n.], 2006. http://webdoc.sub.gwdg.de/diss/2006/andronesi.
Повний текст джерелаAbd, Rahim Munirah Sufiyah [Verfasser], Sonja A. [Akademischer Betreuer] Dames, Bernd [Gutachter] Reif, and Sonja A. [Gutachter] Dames. "Characterization of the structure, dynamics and immersion properties of the membrane-associating FATC domain of ataxia telangiectasia mutated by solution NMR spectroscopy and complementary methods / Munirah Sufiyah Abd Rahim ; Gutachter: Bernd Reif, Sonja A. Dames ; Betreuer: Sonja A. Dames." München : Universitätsbibliothek der TU München, 2019. http://d-nb.info/1182536360/34.
Повний текст джерелаLundborg, Magnus. "Computer-Assisted Carbohydrate Structural Studies and Drug Discovery." Doctoral thesis, Stockholms universitet, Institutionen för organisk kemi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-56411.
Повний текст джерелаAt the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 4: Submitted. Paper 5: Manuscript. Paper 6. Manuscript.
Rodgers, Christopher T. "Magnetic field effects in chemical systems." Thesis, University of Oxford, 2007. http://ora.ox.ac.uk/objects/uuid:f5878b88-c5ba-4cbd-83af-857431aef66e.
Повний текст джерела