Thèses sur le sujet « Proteins - Conformation Dynamics »
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Ceres, Nicoletta. « Coarse-grain modeling of proteins : mechanics, dynamics and function ». Thesis, Lyon 1, 2012. http://www.theses.fr/2012LYO10030.
Texte intégralProteins are flexible molecules, which accomplish a variety of cellular tasks through mechanical motions and conformational fluctuations encoded in their three-dimensional structure. Amongst the theoretical approaches contributing to a better understanding of the relationship between protein structure, mechanics, dynamics and function, coarse-grain models are a powerful tool. They can be used to integrate structural and dynamic information over broad time and size scales at a low computational cost, achieved by averaging out the less important degrees of freedom. In this work, fast comparative studies of protein flexibility and mechanics have been performed with the simple coarse-grain Elastic Network Model. However, the dependency of the results on the starting conformation, and the rather constrained backbone dynamics imposed by the harmonic approximation, motivated the development of a new approach, for a more extensive exploration of conformational space. These efforts led to the PaLaCe model, designed to allow significant changes in secondary structure, while maintaining residue specificity despite a lower-level resolution. Using PaLaCe, we were able to reproduce two processes involving protein plasticity: the mechanical unfolding of the I27 domain of the giant muscle protein titin and the near-native dynamics of two homologous enzymes adapted to work at different temperatures. Agreement with experimental data and results from published atomistic models demonstrate that PaLaCe is a reliable, sufficiently accurate, but computationally inexpensive approach. It therefore opens the doors for a systematic investigation of the link between protein dynamics/mechanics and function
Kragelj, Jaka. « Structure and dynamics of intrinsically disordered regions of MAPK signalling proteins ». Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV060/document.
Texte intégralProtein signal transduction pathways allow cells respond to and process signals from the environment. A group of such pathways, called mitogen-activated protein kinase (MAPK) signal transduction pathways, is well conserved in all eukaryotic cells and is involved in regulating many important cell processes. Long intrinsically disordered region (IDRs), present in many MAPKs, have remained structurally uncharacterised. The IDRs of MAPKs are especially important as they contain docking-site motifs which control the interactions between MAPK proteins themselves and also between MAPKs and other interacting proteins containing the same motifs. Nuclear magnetic resonance (NMR) spectroscopy in combination with other biophysical techniques was used to study IDRs of MAPKs. NMR spectroscopy is well suited for studying intrinsically disordered proteins (IDPs) at atomic-level resolution. NMR observables, such as for example chemical shifts and residual dipolar couplings, can be used together with ensemble selection methods to study residual structure in IDRs. Nuclear spin relaxation informs us about fast pico-nanosecond motions. NMR titrations and exchange spectroscopy techniques can be used to monitor kinetics of protein-protein interactions. The mechanistic insight into function of IDRs and motifs will contribute to understanding of how signal transduction pathways work
Murzycki, Jennifer E. « Probing Protein Dynamics Through Mutational and Computational Studies of HIV-1 Protease : A Dissertation ». eScholarship@UMMS, 2006. https://escholarship.umassmed.edu/gsbs_diss/166.
Texte intégralAbyzov, Anton. « Nuclear Magnetic Resonance Studies of the Dynamics and Thermodynamics of Intrinsically Disordered Proteins ». Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAY026/document.
Texte intégralIntrinsically disordered proteins (IDPs) are highly flexible heteropolymers, implicated in important cellular activities (signal transduction, molecular recognition, transcription, translation, etc.) and representing potential drug targets against cancer and neurodegenerative diseases, whose dynamic modes define their biological function. Although the conformational states sampled by IDPs are relatively well understood, essentially nothing is known about the associated dynamic timescales. In this study we investigate the conformational behavior of the intrinsically disordered C-terminal domain of the nucleoprotein of Sendai virus (NTAIL), which interacts with the PX domain of the phosphoprotein. The interaction site has been shown to sample an equilibrium of discrete helices in the free state, which forms an encounter complex implicating the stabilization of one of the helical conformers upon interaction with PX, prior to diffusing on the surface of PX and engaging in the actual binding site. However, very little is known about the timescales of chain motions, which surely play a role in the interaction kinetics, in particular in terms of the on-rate of the interaction. This 124 amino acid protein also provides a good model system, containing long unfolded domains with chain-like dynamics and regions with residual structure. The measurement of extensive set of coherent relaxation rates at multiple magnetic fields, multiple temperatures and in three different length constructs of the same IDP has allowed us to characterize the dynamic nature of NTAIL in unprecedented detail. By analyzing the relaxation data using extended model-free approach, we show that fast (≤ 50 ps) components of the correlation function report on librational motions. A dominant mode occurs on timescales around one nanosecond, apparently reporting on backbone sampling within Ramachandran sub-states, while a slower component (5-25 ns) reports on segmental dynamics dominated by the chain-like nature of the protein. The ability to delineate intrinsic modes and timescales will improve our understanding of the behavior and function of IDPs
Link, Justin J. « Ultrafast Protein Conformation Dynamics ». The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1230584570.
Texte intégralDorywalska, Magdalena. « Conformational dynamics of protein synthesis / ». May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.
Texte intégralZang, Chen. « Ultrafast Spectroscopic Study of Protein Conformation Dynamics and Hydration Dynamics ». The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1299481658.
Texte intégralBossa, Cecilia. « Conformational fluctuations in proteins. A molecular dynamics based study ». Doctoral thesis, La Sapienza, 2005. http://hdl.handle.net/11573/916821.
Texte intégralChen, Wei. « Molecular dynamics simulations of binding, unfolding, and global conformational changes of signaling and adhesion molecules ». Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/28118.
Texte intégralCommittee Chair: Zhu, Cheng; Committee Member: Harvey, Stephen; Committee Member: Hud, Nicholas; Committee Member: Zamir, Evan; Committee Member: Zhu, Ting.
Bruce, Neil John. « Investigating protein conformational change via molecular dynamics simulation ». Thesis, University of Manchester, 2011. https://www.research.manchester.ac.uk/portal/en/theses/investigating-protein-conformational-change-via-molecular-dynamics-simulation(17145939-f643-4b23-bbb9-029cf5489c15).html.
Texte intégralD'Rozario, Robert S. G. « Conformational dynamics of proline-containing transmembrane helices ». Thesis, University of Oxford, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.670181.
Texte intégralBudi, Bunarta Hendra (Akin), et akin budi@rmit edu au. « On the effects of external stresses on protein conformation ». RMIT University. School of Applied Sciences, 2006. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20061116.123431.
Texte intégralReiner, Andreas. « Conformational dynamics and stability of structured peptides and small proteins / ». Basel : [s.n.], 2009. http://edoc.unibas.ch/diss/DissB_8562.
Texte intégralAnderson, William David. « Conformational dynamics of interleukin-1beta and protein-membrane interactions ». Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2007. http://wwwlib.umi.com/cr/ucsd/fullcit?p3249669.
Texte intégralTitle from first page of PDF file (viewed April 4, 2007). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 119-127).
Bransford, Philip W. « Insights into protein function from evolutionary and conformational dynamics ». Thesis, Massachusetts Institute of Technology, 2011. http://hdl.handle.net/1721.1/76112.
Texte intégralCataloged from PDF version of thesis.
Includes bibliographical references (p. 125-144).
The volume of protein structure data has grown rapidly over the past 30 years, leaving a wake of facts that still require explanation. We endeavored to answer a few open questions on the structure-function relationship of intriguing mechanochemical protein systems. To this end this thesis work contains five studies that offer novel insights into molecular biomechanical systems that may guide future basic research or applications development. The first study concerns the biophysics of cadherin-mediated cell sorting observed in developing solid tissue. We investigated the evolutionary dynamics of the cadherin superfamily of cell-cell adhesion proteins to infer a structural basis for their paradoxical mixture of pairwise binding specificity and promiscuity. Our analysis predicts a small set of specificity-determining residues located within the protomer-protomer binding interface. The putative specificity-determinants form a design space with potential for engineering novel cell-cell adhesive interactions. The second study addresses the open question of how to automatically identify regions within a protein that engage in allosteric communication. To identify allostery we developed and tested two computational tools that operate on protein conformational dynamics data. These tools are useful for generating testable hypotheses about proteins with multiple functional sites for the design of non-competitive protein inhibitors. The third study asks, "What is the consequence of allosteric cooperation between the tandem binding sites in a class of proteins that bundle filamentous actin (F-actin)?" Through simulation we demonstrate that cooperative F-actin bundling tends to strengthen bundles by driving the formation of cross-links between neighboring filaments while depleting F-actin binding sites that are occupied but not cross-linked. We hence propose that allostery may be a natural feature of ABPs with tandem F-actin binding sites if nature indeed selects for sturdy F-actin bundles. The final two studies examine the impact of two structural perturbations to Factin on its mechanics. Using structure-based computer modeling we develop a simple explanation for the mechanism by which the structure of actin's polymorphic subdomain 2 mediates 4-fold changes in F-actin's flexibility. We further demonstrate that two calponin homology domains stabilize F-actin by binding in a configuration that tends to relax the stress concentration at actin-actin interfaces.
by Philip W. Bransford.
Ph.D.
Stone, Benjamin. « Evaluating experimental and theoretical measures of protein conformational dynamics ». Thesis, Aston University, 2016. http://publications.aston.ac.uk/31759/.
Texte intégralZhou, Guangfeng. « STATISTICAL MODELS AND THEIR APPLICATIONS IN STUDYING BIOMOLECULAR CONFORMATIONAL DYNAMICS ». Diss., Temple University Libraries, 2017. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/478773.
Texte intégralPh.D.
It remains a major challenge in biophysics to understand the conformational dynamics of biomolecules. As powerful tools, molecular dynamics (MD) simulations have become increasingly important in studying the full atomic details of conformational dynamics of biomolecules. In addition, many statistical models have been developed to give insight into the big datasets from MD simulations. In this work, I first describe three statistical models used to analyze MD simulation data: Lifson-Roig Helix-Coil theory, Bayesian inference models, and Markov state models. Then I present the applications of each model in analyzing MD simulations and revealing insight into the conformational dynamics of biomolecules. These statistical models allow us to bridge microscopic and macroscopic mechanisms of biological processes and connect simulations with experiments.
Temple University--Theses
Atzori, Alessio. « Conformational analysis of peptides and proteins for drug design using molecular simulations ». Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/conformational-analysis-of-peptides-and-proteins-for-drug-design-using-molecular-simulations(050ba296-a4c4-4a5b-87bf-66d90f7ddc5a).html.
Texte intégralCao, Jin. « Single Molecular Spectroscopy and Atomic Force Manipulation of Protein Conformation and Dynamics ». Bowling Green State University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1416588612.
Texte intégralLópez, Asamar Abraham. « Study of the conformational dynamics of prolyl oligopeptidase ». Doctoral thesis, Universitat de Barcelona, 2015. http://hdl.handle.net/10803/301430.
Texte intégralLa prolil oligopeptidasa (POP) es un enzim de 81 KDa que hidrolitza pèptids curts amb contingut en prolina. La POP actua en el sistema nerviós central mitjançant interaccions proteïna-proteïna (IPP), i la seva funció biològica està relacionada amb la memòria i els processos cognitius. Per aquesta raó, els inhibidors de la POP són compostos d’interès terapèutic per al tractament dels dèficits cognitius. Recentment, s’ha descobert que els inhibidors de la POP poden prevenir la patogènesis de la malaltia de Pàrkinson, probablement a través d’una interacció directa entre la POP i l’a-sinucleïna (la principal proteïna causant dels processos neurodegeneratius de la malaltia de Parkinson). Tot i que l’estructura cristal·logràfica de la POP està ben definida, no es sap quines són les transicions conformacionals que permeten completar el cicle catalític de la POP. Probablement, aquesta riquesa conformacional també té un paper rellevant en el control de les IPP. Malauradament, l’estudi conformacional complet de la POP és tot un repte degut al seu elevat pes molecular. En aquesta tesis doctoral s’ha emprat una combinació de tècniques biofísiques avançades (en concret, la resonància magnètica nuclear, la dispersió de raigs X de baix angle, i l’espectrometria de masses de mobilitat iònica) conjuntament amb simulacions de dinàmica molecular, per tal d’analitzar la dinàmica conformacional de la POP en solució. A més, s’ha estudiat la possible interacció entre la POP i l’a-sinucleïna mitjançant experiments de RMN. Els resultats obtinguts en aquesta tesi doctoral han demostrat que la POP es troba en solució en un equilibri conformacional lent entre conformacions obertes i tancades, originades a partir de la separació entre dos dominis. Els inhibidors de la POP causen una gran estabilització de la conformació tancada, amb la qual cosa l’equilibri dinàmic es desplaça totalment cap a aquesta conformació. A més, es va poder detectar una interacció dèbil i transitòria entre la POP i l’a-sinucleïna, que esdevenia especialment afavorida en la presència d’inhibidors. Així, els nostres resultats suggereixen que la diversitat conformacional de la POP es necessària per a la seva funció, i que els inhibidors poden desencadenar la seva funció biològica desplaçant l’equilibri conformacional.
Jones, Kevin C. (Kevin Chapman). « Temperature-jump 2D IR spectroscopy to study protein conformational dynamics ». Thesis, Massachusetts Institute of Technology, 2012. http://hdl.handle.net/1721.1/73358.
Texte intégral"June 2012." Cataloged from PDF version of thesis.
Includes bibliographical references.
Temperature-jump (T-jump) two-dimensional infrared spectroscopy (2D IR) is developed, characterized, and applied to the study of protein folding and association. In solution, protein conformational changes span a wide range of timescale from nanoseconds to minutes. Ultrafast 2D IR spectroscopy measures time-dependent structural changes within the protein ensemble by probing the frequency changes associated with amide I backbone vibrations. Combining 2D IR with a perturbing laser-induced T-jump enables the study of conformational dynamics from 5 ns to 50 ms. To access a finer time-sampling of the conformational evolution, a one-dimensional variant of 2D IR, heterodyne-detected dispersed vibrational echo spectroscopy (HDVE), is implemented. The framework for interpreting transient HDVE and 2D IR spectra is developed, and we propose a method to remove the linear absorption distortions along both frequency axes. We first present the T-jump 2D IR spectra of a dipeptide to reveal the general amide I baseline response expected in the absence of conformational change. To facilitate the analysis of T-jump data, singular value decomposition (SVD) is employed for reducing noise, identifying the number of distinguishable states, and separating spectral changes based on shared timescales. Finally, T-jump 2D IR spectroscopy is applied to study the unfolding of ubiquitin, disordering of the 12-residue p-hairpin peptide trpzip2 (TZ2), and the dissociation of insulin dimers to monomers. Experimental results for ubiquitin highlight the importance of linear absorption corrections for interpretation of the data. In response to the T-jump, 2D IR results indicate p-sheet structure melts in ubiquitin with a small amplitude (~10 gs) and large amplitude (17 ms) response. Isotope-labeling T-jump experiments on TZ2 allow for the proposal of a free energy surface in which transitions from a native and misfolded state proceed through a disordered hub-like state with a 1-2 gs timescale. Multiple timescales are observed in the T-jump induced dissociation of insulin. Based on their spectral features and concentration dependence, the insulin timescales can be assigned to dissociation, disordering, and oligomerization processes. With these applications, we demonstrate the capability of T-jump 2D IR spectroscopy to reveal detailed molecular dynamics.
by Kevin C. Jones.
Ph.D.
Chatterjee, P. « Protein thermal stability, conformational dynamics and solvent properties : insights with atomistic molecular dynamics simulations ». Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2015. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/2242.
Texte intégralGillespie, D. Blake. « Conformational dynamics and intermediates in the folding pathway of T4 lysozyme / ». view abstract or download file of text, 1999. http://wwwlib.umi.com/cr/uoregon/fullcit?p9957566.
Texte intégralTypescript. Includes vita and abstract. Includes bibliographical references (leaves 101-110). Also available for download via the World Wide Web; free to University of Oregon users. Address: http://wwwlib.umi.com/cr/uoregon/fullcit?p9957566.
Majumdar, Devdoot. « Probing the conformational dynamics of membrane-associated proteins using single molecule fluorescence ». Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1973051401&sid=3&Fmt=2&clientId=1564&RQT=309&VName=PQD.
Texte intégralLukman, Suryani. « The functional significance of the conformational dynamics of monomeric and multimeric proteins ». Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609894.
Texte intégralMenon, S. « Triggers for protein conformational changes and self-assembly probed with fully atomistic computer simulations ». Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2019. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/5845.
Texte intégralKarolak, Aleksandra. « Application and Development of Computational Methods in Conformational Studies of Bio-molecules ». Scholar Commons, 2015. https://scholarcommons.usf.edu/etd/5520.
Texte intégralHibbs, Ryan E. « Conformational dynamics of the acetylcholine binding protein, a Nicotinic receptor surrogate ». Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2006. http://wwwlib.umi.com/cr/ucsd/fullcit?p3237010.
Texte intégralTitle from first page of PDF file (viewed December 8, 2006). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
Wan, Hongbin. « Efficient sampling of protein conformational dynamics and prediction of mutation effects ». Diss., Temple University Libraries, 2019. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/575951.
Texte intégralPh.D.
Molecular dynamics (MD) simulation is a powerful tool enabling researchers to gain insight into biological processes at the atomic level. There have been many advancements in both hardware and software in the last decade to both accelerate MD simulations and increase their predictive accuracy; however, MD simulations are typically limited to the microsecond timescale, whereas biological motions can take seconds or longer. Because of this, it remains extremely challenging to restrain simulations using ensemble-averaged experimental observables. Among various approaches to elucidate the kinetics of molecular simulations, Markov State Models (MSMs) have proven their ability to extract both kinetic and thermodynamic properties of long-timescale motions using ensembles of shorter MD simulation trajectories. In this dissertation, we have implemented an MSM path-entropy method, based on the idea of maximum-caliber, to efficiently predict the changes in protein folding behavior upon mutation. Next, we explore the accuracy of different MSM estimators applied to trajectory data obtained by adaptive seeding, in which new rounds of short MD simulations are collected from states of interest, and propose a simple method to build accurate models by population re-weighting of the transition count matrix. Finally, we explore ways to reconcile simulated ensembles with Hydrogen/Deuterium exchange (HDX) protection measurements, by constructing multi-ensemble Markov State Models (MEMMs) from biased MD simulations, and reconciling these predictions against the experimental data using the BICePs (Bayesian Inference of Conformational Populations) algorithm. We apply this approach to model the native-state conformational ensemble of apomyoglobin at neutral pH.
Temple University--Theses
Guan, Xiao, et 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.
Texte intégralGuo, Qing. « Single Molecule Optical Magnetic Tweezers Microscopy Studies of Protein Dynamics ». Bowling Green State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1435334948.
Texte intégralZhang, Wei. « Computational simulation of biological systems studies on protein folding and protein structure prediction / ». Access to citation, abstract and download form provided by ProQuest Information and Learning Company ; downloadable PDF file 2.84Mb, 184 p, 2005. http://wwwlib.umi.com/dissertations/fullcit/3181881.
Texte intégralGuan, Xiao. « NMR approaches to protein conformation and backbone dynamics studies on hyperthermophilic acylphosphatase and neuropeptide secretoneurin / ». Click to view the E-thesis via HKUTO, 2010. http://sunzi.lib.hku.hk/hkuto/record/B44079230.
Texte intégralTamura, Kouichi. « Atomistically Deciphering Functional Large Conformational Changes of Proteins with Molecular Simulations ». 京都大学 (Kyoto University), 2016. http://hdl.handle.net/2433/215334.
Texte intégralAstudillo, Luisana. « Conformational Dynamics Associated with Ligand Binding to Vertebrate Hexa-coordinate Hemoglobins ». FIU Digital Commons, 2014. http://digitalcommons.fiu.edu/etd/1177.
Texte intégralAhlstrom, Logan Sommers. « Molecular Dynamics Simulation of the Effect of the Crystal Environment on Protein Conformational Dynamics and Functional Motions ». Diss., The University of Arizona, 2012. http://hdl.handle.net/10150/255200.
Texte intégralCraigo, Kevin Alan. « Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin ». The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1311089745.
Texte intégralMiyashita, Osamu. « ROLE OF CONFORMATIONAL DYNAMICS ON ELECTRON AND ENERGY TRANSFER IN A PROTEIN MOLECULE ». 京都大学 (Kyoto University), 2000. http://hdl.handle.net/2433/151675.
Texte intégralKim, So Yeon. « Observing protein dynamics and conformational changes by ensemble and single-molecule fluorescence spectroscopy / ». May be available electronically:, 2008. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.
Texte intégralPao, Ya-Lan. « Conformational and dynamic studies of the influence of glycosylation on peptides and proteins ». Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285416.
Texte intégralChan, Yao Chong Maud. « Structure et dynamique de protéines intrinsèquement désordonnées : Caractérisation par une approche combinant dynamique moléculaire avancée et SAXS ». Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS257.
Texte intégralThe PhD work will consist in exploring and characterizing the conformational ensemble of intrinsically disordered proteins (IDPs), by using several complementary methods, including enhanced molecular dynamics simulations and small angle X-ray scattering (SAXS). IDPs are proteins having one or several regions that lack stable secondary structures in the unbound state, but which can adopt various structured conformations to bind other proteins. In the case of three IDPs, the project aims to answer the question of whether these secondary structures formed at the protein-protein interfaces transiently pre-exist or not in the unbound state of solvated IDPs. If it is possible to identify and characterize these molecular recognition features (MoRFs) in the IDP unbound state, then the results of this work will subsequently help to determine the structures of protein complexes involving IDPs
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.
Texte intégralHeil, Christina Sabine [Verfasser], Martin [Gutachter] Grininger et Michael [Gutachter] Göbel. « Towards the conformational dynamics of multidomain proteins / Christina Sabine Heil ; Gutachter : Martin Grininger, Michael Göbel ». Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2019. http://d-nb.info/1198932856/34.
Texte intégralWang, Zijian. « Single-Molecule Spectroscopy And Imaging Studies Of Protein Folding-Unfolding Conformational Dynamics : The Multiple-State And Multiple-Channel Energy Landscape ». Bowling Green State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1459942296.
Texte intégralMurciano, Brice. « Dynamique conformationnelle chez les protéines d'adhésion de Babesia : mythe ou réalité ? » Thesis, Montpellier 1, 2013. http://www.theses.fr/2013MON13510/document.
Texte intégralOne of the most common parasitic infections in animals worldwide is babesiosis or piroplasmosis. Caused by the intraerythrocytic development of Babesia parasite, it has many clinical signs similar to those of malaria. This parasite of the phylum Apicomplexa, is transmitted via the tick vector and performs its reproductive cycle in red blood cells of the vertebrate host. B. In Europe divergens and B. canis species are mainly responsible respectively for bovine babesiosis and canine babesiosis. A strategy of vaccine research, the study of parasite proteins in contact with the bloodstream is essential for understanding host-parasite interactions and identify vaccine candidates with high potential. Anchored protein GPI (glycosylphosphatidylinositol) are part of these proteins. The first protein GPI anchors described in B. divergens is Bd37.1. It induces complete protection against infection with B. divergens provided a hydrophobic sequence is added at the C-terminus. Resolution NMR structure of this protein has highlighted a probable mechanism of conformational change as a function of pH. The structure consists of three sub areas shows that it is only maintained by salt bridges which can break in acidic medium. However, the environment within which Bd37.1 membrane anchored to the surface of the parasite and / or approach the red blood cell during the invasion is acidic. This conformational dynamics of the protein-Δ Bd37 linked to the membrane environment, could be at the origin of the mechanism that confers immunity depending on the presence or absence of the hydrophobic sequence at the C-terminus of Bd37.1. We sought to assess the implications of such dynamics in host-parasite interactions through structural study of two parasite proteins (Bd37.1 and Bc28.1). In the first case we study the conformational dynamics of the adhesion protein Bd37.1. We explored the different conformations that may be adopted by a protein Bd37.1 biophysical approach and we have stabilized in different conformations in solution through mutations to study. Among these mutants, the mutant Δ-Bd37-EDK including salt bridges were broken shows different characteristics Δ-Bd37. The data on this mutant led us to solve the structure and to test its power vaccinating. In a second part, we characterize biochemically and functionally Bc28.1 another protein, the ortholog Bd37.1. in B. canis, accompanied with the resolution of its structure. We show that Bc28.1 is an adhesion protein localized to the parasite surface and compare the structures and Bd37.1 Bc28.1. These two structures are ultimately very different while location and function are similar
Foo, Alexander. « New Insights into the Role of Membrane Interactions and Conformational Dynamics in Intramembrane Proteolysis by GlpG Rhomboid ». Thesis, Université d'Ottawa / University of Ottawa, 2017. http://hdl.handle.net/10393/36941.
Texte intégralHassan, Anwar I. « Development of ¹⁹F NMR Methods for the Study of GlpG Rhomboid Protease in Detergents and Lipid Nanoparticle Systems ». Thesis, Université d'Ottawa / University of Ottawa, 2021. http://hdl.handle.net/10393/42521.
Texte intégralHaselbach, David [Verfasser], Holger [Akademischer Betreuer] Stark et Kai [Akademischer Betreuer] Tittmann. « Conformational Dynamics of large protein Complexes / David Haselbach. Gutachter : Holger Stark ; Kai Tittmann. Betreuer : Holger Stark ». Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2015. http://d-nb.info/1067626468/34.
Texte intégralSubramaniam, 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.
Texte intégralBurnley, B. Tom. « New tools to study the conformational dynamics of large proteins : A study of FBP-aldolase and other enzymes ». Thesis, University of Leeds, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.485182.
Texte intégral