Teses / dissertações sobre o tema "Complex pore structure"
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Dvoyashkin, Muslim, Alexey Khokhlov, Rustem Valiullin, Jörg Kärger e Matthias Thommes. "Fluid behavior in porous silicon channels with complex pore structure". Universitätsbibliothek Leipzig, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-190953.
Texto completo da fonteDvoyashkin, Muslim, Alexey Khokhlov, Rustem Valiullin, Jörg Kärger e Matthias Thommes. "Fluid behavior in porous silicon channels with complex pore structure". Diffusion fundamentals 11 (2009) 80, S. 1-2, 2009. https://ul.qucosa.de/id/qucosa%3A14045.
Texto completo da fonteKelich, Joseph M. "Single-Molecule Studies on Nuclear Pore Complex Structure and Function". Diss., Temple University Libraries, 2018. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/511772.
Texto completo da fontePh.D.
Nuclear pore complexes (NPCs) are large macromolecular gateways embedded in the nuclear envelope of Eukaryotic cells that serve to regulate bi-directional trafficking of particles to and from the nucleus. NPCs have been described as creating a selectively permeable barrier mediating the nuclear export of key endogenous cargoes such as mRNA, and pre-ribosomal subunits as well as allow for the nuclear import of nuclear proteins and some viral particles. Remarkably, other particles that are not qualified for nucleocytoplasmic transport are repelled from the NPC, unable to translocate. The NPC is made up of over 30 unique proteins, each present in multiples of eight copies. The two primary protein components of the NPC can be simplified as scaffold nucleoporins which form the main structure of the NPC and the phenylalanine-glycine (FG) motif containing nucleoporins (FG-Nups) which anchor to the scaffold and together create the permeability barrier within the pore. Advances in fluorescence microscopy techniques including single-molecule and super-resolution microscopy have made it possible to label and visualize the dynamic components of the NPC as well as track the rapid nucleocytoplasmic transport process of importing and exporting cargoes. The focus of this dissertation will be on live cell fluorescence microscopy application in probing the dynamic components of the NPC as well as tracking the processes of nucleocytoplasmic transport.
Temple University--Theses
Nordeen, Sarah Ann. "A nanobody suite for yeast scaffold nucleoporins provides details of the Y complex structure and nuclear pore complex assembly". Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/127138.
Texto completo da fonteCataloged from the official PDF of thesis.
Includes bibliographical references.
Nuclear pore complexes (NPCs) are the main conduits for molecular exchange across the nuclear envelope. The NPC is a modular assembly of ~500 individual proteins, called nucleoporins or nups, that can be classified into three categories: 1. Stably associated scaffolding nups, 2. Peripheral nups, and 3. Phenylalanine-glycine (FG) repeat containing nups that form the permeability barrier of the NPC. Most scaffolding nups are organized in two multimeric subcomplexes, the Nup84 or Y complex and the Nic96 complex. Working in S. cerevisiae to study the assembly of these two essential subcomplexes, we developed a suite of twelve nanobodies that recognize seven constituent nucleoporins of the Y and Nic96 complexes. The nanobodies bind their targets specifically and with high affinity, albeit with varying kinetics. We mapped the epitope of eight members of the nanobody library via crystal structures of nup-nanobody co-complexes.
Nuclear pore complexes (NPCs) are the main conduits for molecular exchange across the nuclear envelope. The NPC is a modular assembly of ~500 individual proteins, called nucleoporins or nups, that can be classified into three categories: 1. Stably associated scaffolding nups, 2. Peripheral nups, and 3. Phenylalanine-glycine (FG) repeat containing nups that form the permeability barrier of the NPC. Most scaffolding nups are organized in two multimeric subcomplexes, the Nup84 or Y complex and the Nic96 complex. Working in S. cerevisiae to study the assembly of these two essential subcomplexes, we developed a suite of twelve nanobodies that recognize seven constituent nucleoporins of the Y and Nic96 complexes. The nanobodies bind their targets specifically and with high affinity, albeit with varying kinetics. We mapped the epitope of eight members of the nanobody library via crystal structures of nup-nanobody co-complexes.
In two cases, the nanobodies facilitated the crystallization of novel nup structures, namely the full-length Nup84-Nup133 [alpha]-helical domain structure and the Nup133 [beta]-propeller domain structure. Together these two structures completely characterize the S. cerevisiae Y complex molecular assembly. Further, the Nup133 [beta]-propeller domain contains a structurally conserved amphipathic lipid packing sensor (ALPS) motif thought to anchor the Y complex to the nuclear envelope, which we confirmed by liposome interaction studies. An additional nanobody facilitated the structure of Nic96 at an improved resolution, revealing previously missing helices. In addition to the utility of these nanobodies for in vitro characterization of NPC assemblies, we also show that expression of nanobody-fluorescent protein fusions reveals details of the NPC assembly in their native, in vivo environment, and possibly of NPC heterogeneity within the nuclear envelope.
Overall, this suite of nanobodies provides a unique and versatile toolkit for the study of the NPC.
by Sarah Ann Nordeen.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Biology
Raneri, Simona. "Complex Pore Geometries in Natural Building Stones: an experimental and theoretical approach for the modeling of porosity changes in natural, degraded and treated calcarenites". Doctoral thesis, Università di Catania, 2016. http://hdl.handle.net/10761/4021.
Texto completo da fonteKelley, Kotaro. "Structural and biochemical characterization of nuclear pore complex structural scaffold sub-complexes". Thesis, Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/113466.
Texto completo da fonteCataloged from PDF version of thesis.
Includes bibliographical references.
The nuclear pore complex (NPC) is a large, modular protein assembly that regulates nucleocytoplasmic transport in all eukaryotes. The ~60-120 MDa NPC is a modular assembly of multiple copies of ~30 distinct proteins that are arranged into biochemically distinct sub-complexes. We believe that the structural characterization of the NPC is essential for understanding its transport mechanisms and various pathologies and human diseases associated with deletions or mutations of constituents. To obtain detailed structural information of the NPC, techniques that span several resolution ranges are necessary due to its large size and complexity. For instance, recent progress in the structural characterization of the overall architecture of the NPC by cryo-electron tomography(cryo-ET) to ~23Å resolution has revealed its size, shape, and course arrangement, but lacks distinguishable protein-protein boundaries and secondary structural details.
Although the entire NPC is not amenable to high resolution X-ray crystallography, we complement the cryo-ET reconstructions with a divide and conquer approach by obtaining high resolution X-ray crystal structures of individual subcomplexes. By taking advantage of the modular nature of the NPC, we can dock subcomplexes into the cryo-ET reconstructions to identify their location within the NPC. This composite structure will bridge the meso resolution cryo-ET reconstructions of the entire NPC and the incomplete but high resolution X-ray crystal structure of individual subcomplexes. As a first step towards understanding the detailed organization of the NPC, our goal is to solve the high resolution structures of the two principal structural scaffold subcomplexes, the Y and Nic96 complexes. In this study, we present the high resolution composite X-ray crystal structure of the Y complex.
Docking the composite model into previously solved random conical tilt(RCT) and tomographic reconstructions of negatively stained samples of the Y complex shows overall consistency between the three methods, yet we highlight important structural differences that constrain possible arrangements of multiple Y complexes within the NPC. By docking the composite model into the cryo-ET reconstructions of the entire NPC, we propose an arrangement of multiple Y complexes that is consistent with our composite structure. In addition, progress on structurally characterizing the Nic96 complex will be presented. Preliminary results suggest that Nup1 92 and Nic96 form a flexible, yet semi-ordered interface. Future directions for characterizing the rest of the Nic96 complex, including current challenges and suggestions will be discussed.
by Kotaro Kelley.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Biology
Chemudupati, Mahesh. "Investigating the effects of nuclear envelope proteins on nuclear structure and organization in Aspergillus nidulans". The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu148009978216118.
Texto completo da fonteYacouba, Amani Abdoul Nasser. "Approche multi-géophysique pour la caractérisation de la fracturation et des propriétés de transport des roches carbonatées". Electronic Thesis or Diss., Orléans, 2024. http://www.theses.fr/2024ORLE1024.
Texto completo da fonteIn a context of global changes and ecological and energy transitions, climate change induces recurrent drought and water resource crisis in several regions and continents. It is crucial to study groundwaters in order to support these transitions and ensure effective management and use of this vital resource. In particular, the vadose zone which plays an important role in the recharge of these groundwaters and the transfer of possible pollutants and inputs. Most of the time this unsaturated zone is characterized by multi-scale heterogeneities (e.g., pore structure, fractures, mineralogical variation) particularly in a limestone environment. These heterogeneities are complexified by diagenetic processes linked mainly to physicochemical and mineralogical alteration which leads to uncertainty in reservoir property (e.g., porosity, permeability, water saturation) estimation from geophysical methods. Among these methods, acoustic and electrical methods are well suited because of the strong relation between heterogeneities and the measured properties.This thesis relies on a multi-geophysical approach in order to better characterize a complex carbonate reservoir using petrophysical measurements combined with microstructural descriptions. Based on this approach, we demonstrated the influence of rock structure on the prediction and modeling of petroacoustic properties. This work leads to a good discrimination of some facies, which can be used to improve simulation and flow models. In addition, we demonstrate the relevance of complex conductivity measurements in limestone characterization and permeability prediction. However, additional developments are needed to understand the upscaling problematic for heterogeneous and complex reservoirs
Walther, Tobias. "The role of Peripheral Nuclear Pore Complex (NPC) structures in nuclear transport and NPC architecture". Diss., lmu, 2002. http://nbn-resolving.de/urn:nbn:de:bvb:19-4945.
Texto completo da fontePartridge, James R. (James Robert). "Biophysical and structural characterization of components from the nuclear pore complex and the ubiquitin pathway". Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/57994.
Texto completo da fonteCataloged from PDF version of thesis.
Includes bibliographical references (p. 136-151).
Formation of an endomembrane system in the eukaryotic cell is a hallmark of biological evolution. One such system is the nuclear envelope (NE), composed of an inner and outer membrane, used to form a nucleus and enclose the cell's genome. Access to the nucleus from the cytoplasm is mediated by a massive macromolecular machine called the nuclear pore complex (NPC). The NPC resides as a circular opening embedded in the NE and is composed of only -30 proteins that assemble with octagonal symmetry as biochemically defined subcomplexes to form the NPC. One such subcomplex is the Nspl / Nup62 complex, composed of three proteins and stabilized by coiled-coil interactions. Here we reconstitute a tetrameric assembly between the Nspl-complex and a fourth nucleoporin (Nup) Nic96. Nic96 harbors a 20 kDa coiled-coil domain at the N-terminus followed by a 65 kDa stacked helical domain. The coiled-coil domain of the Nspl -complex and the N-terminus of Nic96 combine to form a tetrameric assembly, integrated into the NPC lattice scaffold via the stacked helical domain of Nic96. We characterized the coiled-coil assembly with size exclusion chromatography and analytical ultracentrifugation. Deletion experiments and point mutations, directed by hydrophobic cluster analysis, were used to map connecting helices between members of the protein assembly. Although the core of the NPC is a rigid scaffold built for structural integrity, the NPC as a whole is a dynamic macromolecular machine. Protein transport is regulated by the small G protein Ran. Ran interacts with the NPC of metazoa via two asymmetrically localized components, Nupl53 at the nuclear face and Nup358 at the cytoplasmic face. Both Nups contain distinct RANBP2 type zinc finger (ZnF) domains. We present crystallographic data detailing the interaction between Nup1 53-ZnFs and RanGDP. A crystal-engineering approach led to well-diffracting crystals so that all ZnF-Ran complex structures are refined to high resolution. Each of the four zinc finger modules of Nup1 53 binds one Ran molecule in largely independent fashion. Nupl53-ZnFs bind RanGDP with higher affinity than RanGTP, however the modest difference suggests that this may not be physiologically meaningful. ZnFs may be used to concentrate Ran at the NPC to facilitate nucleocytoplasmic transport. In a separate study we present a structural analysis of the HECT domain from the E3 ubiquitin ligase HUWE1 and with biophysical data we show that an N-terminal helix stabilizes the HECT domain. This element modulates activity, as measured by self-ubiquitination induced in the absence of this helix, distinct from its effects on Ub conjugation of substrate Mcl-1. Such subtle structural elements in this domain potentially regulate the variable substrate specificity displayed by all HECT domain type, E3 ubiquitin ligases.
by James R. Partridge.
Ph.D.
Brohawn, Stephen Graf. "Structural elucidation of a common architecture of the nuclear pore complex and COPIl vesicle coats". Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/58396.
Texto completo da fonteCataloged from PDF version of thesis.
Includes bibliographical references (p. 156-169).
Nuclear pore complexes (NPCs) are massive protein assemblies that perforate the nuclear envelope and form the exclusive passageway for nucleocytoplasmic transport. NPCs play critical roles in molecular transport and a myriad of other cellular processes. Elucidation of the structure of the NPC is thus expected to provide important insight into cell biology. In this thesis, I investigate the structure of a key subcomplex of the NPC and discuss the evolutionary relationship between the NPC and COPIl vesicle coats it illustrates. The NPC is a modular assembly, with a stable structural scaffold supporting dynamically attached components. The structural scaffold is constructed from multiple copies of the Y-shaped complex and the Nic96 complex. We solved the crystal structure of the heterodimeric Nup85-Sehl module that forms a short arm in the Y complex. Nup85 is found to contain a conserved fold, the ancestral coatomer element 1 (ACE1), also present in three other components of the NPC and in the COPI vesicle coat, providing structural evidence of coevolution from a common ancestor. Sec3l ACE1 units interact to form edge elements in the COPI lattice. Using structural knowledge of this edge element, we identified corresponding interactions between ACE1 proteins Nup84 and Nup145C in the NPC. We solved the crystal structure of the heterotrimeric Nup84-Nupl 45C-Secl 3 module that forms the top of the long arm in the Y complex. The heterotypic ACE1 interaction of Nup145C and Nup84 is analogous to the homotypic Sec31 edge element interaction in the COPIl coat. From these and other structures, we assemble a near complete structural model of the Y complex. Further, based on the demonstrated relationship with the COPIl coatomer lattice, we propose a lattice model for the entire NPC scaffold. The common architectural principles of the edge elements in the NPC and COPI lead us to predict that Y complexes will be arranged as struts in the NPC lattice. In this manner, Nup84-Nup145C edge elements are arranged parallel to the transport axis to stabilize the positively curved nuclear envelope. From a lattice model of the NPC follow hypotheses for how other components are integrated into and function within the NPC.
by Stephen Graf Brohawn.
Ph.D.
Pignol, David. "Structures cristallines de la sous-unité III du complexe procarboxypeptidase A-S6 de boeuf et du zymogène de porc : une nouvelle classe de zymogènes ?" Université Joseph Fourier (Grenoble ; 1971-2015), 1994. http://www.theses.fr/1994GRE10082.
Texto completo da fonteDulina, I. O., T. F. Lobunets e A. V. Ragulya. "Relationships Between Pore Structure, Free Carbon Content, Particle Size Distribution and Deposition Stage of Ni/NiO Nanopowers". Thesis, Sumy State University, 2015. http://essuir.sumdu.edu.ua/handle/123456789/42718.
Texto completo da fonteFarr, Julia Christina [Verfasser], e Berenike [Akademischer Betreuer] Maier. "Structural and functional analysis of the nuclear pore complex in Saccharomyces cerevisiae / Julia Christina Farr ; Betreuer: Berenike Maier". Münster : Universitäts- und Landesbibliothek Münster, 2009. http://d-nb.info/1140917676/34.
Texto completo da fonteLoing, Vianney. "Stéréotomie et vision artificielle pour la construction robotisée de structures maçonnées complexes". Thesis, Paris Est, 2019. http://www.theses.fr/2019PESC1015/document.
Texto completo da fonteThe context of this thesis work is the development of robotics in the construction industry. We explore the robotic construction of complex masonry structures with the help of computer vision. Construction without the use of formwork is an important issue in relation to both productivity on a construction site and the amount of waste generated. To this end, we study topological interlocking masonries and the possibilities they present. The design of this kind of masonry is standard for planar structures. We generalize it to the design of curved structures in a parametrical way, using PQ meshes and the softwares Rhinoceros 3D and Grasshopper. To achieve this, we introduce a set of inequalities to respect in order to have a topological interlocked structure. These inequalities allow us to present a new result. Namely, it is possible to have an assembly of blocks in which each block is interlocked in translation, while having a subset — composed of several of these blocks — that is not interlocked. We also present a prototype of topological interlocking masonry. Its design is based on variable inclination joints, allowing construction without formwork. In parallel, we are studying robust computer vision for unstructured environments like construction sites, in which sensors are vulnerable to dust or could be accidentally jostled. The goal is to estimate the relative pose (position + orientation) of a masonry block with respect to a robot, using only cheap cameras without the need for calibration. Our approach relies on a classification Convolutional Neural Network trained using hundreds of thousands of synthetically rendered scenes with a robot and a block, and randomized parameters such as block dimensions and poses, light, textures, etc, so that the robot can learn to locate the block without being influenced by the environment. The generation of these images is performed with Unreal Engine 4. This method allows us to estimate a block pose very accurately, with only millimetric errors, without using a single real image for training. This is a strong advantage since acquiring representative training data is a long and expensive process. We also built a new rich dataset of real robot images (about 12,000 images) with accurately localized blocks so that we can evaluate our approach and compare it to alternative approaches. A real demonstrator, including a ABB IRB 120 robot, cuboid blocks and three webcams was set up to prove the feasibility of the method
Böhmer, Thomas. "Functional and structural dissection of Nup107 and Nup133, two members of the Nup107-160 subcomplex, linchpin of the vertebrate nuclear pore complex". [S.l. : s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975117866.
Texto completo da fonteDulina, I. O., T. F. Lobunets, L. O. Klochkov e A. V. Ragulya. "Synthesis of Ni/NiO Nanosize Powders with Different Phase Ratio by Thermal Decomposition of Nickel Acetate Amines". Thesis, Sumy State University, 2013. http://essuir.sumdu.edu.ua/handle/123456789/35125.
Texto completo da fonteGaik, Monika [Verfasser], e Ed [Akademischer Betreuer] Hurt. "Structural and Functional Characterization of the Conserved Nup82 Subcomplex Located on the Cytoplasmic Side of the Yeast Nuclear Pore Complex / Monika Gaik ; Betreuer: Ed Hurt". Heidelberg : Universitätsbibliothek Heidelberg, 2015. http://d-nb.info/1180394887/34.
Texto completo da fonteShmykov, Egor. "Sportovní centrum Brno". Master's thesis, Vysoké učení technické v Brně. Fakulta stavební, 2013. http://www.nusl.cz/ntk/nusl-225829.
Texto completo da fonteMiao, Mi. "Analysis of integral membrane protein Pom34p in nuclear pore complex structure and function". Diss., 2007. http://etd.library.vanderbilt.edu/ETD-db/available/etd-03272007-141235/.
Texto completo da fonteNagy, Vivien [Verfasser]. "Structural analysis of an essential core component of the nuclear pore complex / vorgelegt von Vivien Nagy". 2010. http://d-nb.info/1010669753/34.
Texto completo da fonteWalther, Tobias Christian [Verfasser]. "The role of peripheral nuclear pore complex (NPC) structures in nuclear transport and NPC architecture / von Tobias Christian Walther". 2002. http://d-nb.info/965860906/34.
Texto completo da fontePort, Sarah A. "Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-binding Sites Involved in Nucleocytoplasmic Transport". Doctoral thesis, 2015. http://hdl.handle.net/11858/00-1735-0000-0023-9611-C.
Texto completo da fonteBöhmer, Thomas [Verfasser]. "Functional and structural dissection of Nup107 and Nup133, two members of the Nup107-160 subcomplex, linchpin of the vertebrate nuclear pore complex / vorgelegt von Thomas Böhmer". 2005. http://d-nb.info/975117866/34.
Texto completo da fonteJadidi, Tayebeh. "In-silico Modeling of Lipid-Water Complexes and Lipid Bilayers". Doctoral thesis, 2013. https://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2013102111709.
Texto completo da fonte