Bibliographies thématiques / Proteins self-assembly

Littérature scientifique sur le sujet « Proteins self-assembly »

Auteur : Grafiati
Publié le 10 mars 2023

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Articles de revues sur le sujet "Proteins self-assembly"

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van der Linden, Erik, et Paul Venema. « Self-assembly and aggregation of proteins ». Current Opinion in Colloid & ; Interface Science 12, no 4-5 (octobre 2007) : 158–65. http://dx.doi.org/10.1016/j.cocis.2007.07.010.

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Ringler, P. « Self-Assembly of Proteins into Designed Networks ». Science 302, no 5642 (3 octobre 2003) : 106–9. http://dx.doi.org/10.1126/science.1088074.

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Rad, Behzad, Tom Haxton, Seong-Ho Shin, Steve Whitelam et Caroline Ajo-Franklin. « Self Assembly Pathways of Surface-Layer Proteins ». Biophysical Journal 102, no 3 (janvier 2012) : 261a. http://dx.doi.org/10.1016/j.bpj.2011.11.1437.

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Yang, Liulin, Aijie Liu, Shuqin Cao, Rindia M. Putri, Pascal Jonkheijm et Jeroen J. L. M. Cornelissen. « Self-Assembly of Proteins : Towards Supramolecular Materials ». Chemistry - A European Journal 22, no 44 (18 août 2016) : 15570–82. http://dx.doi.org/10.1002/chem.201601943.

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Ren, Huan, Lifang Wu, Lina Tan, Yanni Bao, Yuchen Ma, Yong Jin et Qianli Zou. « Self-assembly of amino acids toward functional biomaterials ». Beilstein Journal of Nanotechnology 12 (12 octobre 2021) : 1140–50. http://dx.doi.org/10.3762/bjnano.12.85.

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Biomolecules, such as proteins and peptides, can be self-assembled. They are widely distributed, easy to obtain, and biocompatible. However, the self-assembly of proteins and peptides has disadvantages, such as difficulty in obtaining high quantities of materials, high cost, polydispersity, and purification limitations. The difficulties in using proteins and peptides as functional materials make it more complicate to arrange assembled nanostructures at both microscopic and macroscopic scales. Amino acids, as the smallest constituent of proteins and the smallest constituent in the bottom-up approach, are the smallest building blocks that can be self-assembled. The self-assembly of single amino acids has the advantages of low synthesis cost, simple modeling, excellent biocompatibility and biodegradability in vivo. In addition, amino acids can be assembled with other components to meet multiple scientific needs. However, using these simple building blocks to design attractive materials remains a challenge due to the simplicity of the amino acids. Most of the review articles about self-assembly focus on large molecules, such as peptides and proteins. The preparation of complicated materials by self-assembly of amino acids has not yet been evaluated. Therefore, it is of great significance to systematically summarize the literature of amino acid self-assembly. This article reviews the recent advances in amino acid self-assembly regarding amino acid self-assembly, functional amino acid self-assembly, amino acid coordination self-assembly, and amino acid regulatory functional molecule self-assembly.
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Henson, Brandon W., Edward M. Perkins, Jonathan E. Cothran et Prashant Desai. « Self-Assembly of Epstein-Barr Virus Capsids ». Journal of Virology 83, no 8 (21 janvier 2009) : 3877–90. http://dx.doi.org/10.1128/jvi.01733-08.

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ABSTRACT Epstein-Barr virus (EBV), a member of the Gammaherpesvirus family, primarily infects B lymphocytes and is responsible for a number of lymphoproliferative diseases. The molecular genetics of the assembly pathway and high-resolution structural analysis of the capsid have not been determined for this lymphocryptovirus. As a first step in studying EBV capsid assembly, the baculovirus expression vector (BEV) system was used to express the capsid shell proteins BcLF1 (major capsid protein), BORF1 (triplex protein), BDLF1 (triplex protein), and BFRF3 (small capsid protein); the internal scaffold protein, BdRF1; and the maturational protease (BVRF2). Coinfection of insect cells with the six viruses expressing these proteins resulted in the production of closed capsid structures as judged by electron microscopy and sedimentation methods. Therefore, as shown for other herpesviruses, only six proteins are required for EBV capsid assembly. Furthermore, the small capsid protein of EBV (BFRF3), like that of Kaposi's sarcoma-associated herpesvirus, was found to be required for assembly of a stable structure. Localization of the small capsid protein to nuclear assembly sites required both the major capsid (BcLF1) and scaffold proteins (BdRF1) but not the triplex proteins. Mutational analysis of BFRF3 showed that the N-terminal half (amino acids 1 to 88) of this polypeptide is required and sufficient for capsid assembly. A region spanning amino acids 65 to 88 is required for the concentration of BFRF3 at a subnuclear site and the N-terminal 65 amino acids contain the sequences required for interaction with major capsid protein. These studies have identified the multifunctional role of the gammaherpesvirus small capsid proteins.
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Wołek, Karol, et Marek Cieplak. « Self-assembly of model proteins into virus capsids ». Journal of Physics : Condensed Matter 29, no 47 (7 novembre 2017) : 474003. http://dx.doi.org/10.1088/1361-648x/aa9351.

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Javid, Nadeem, Sangita Roy, Mischa Zelzer, Zhimou Yang, Jan Sefcik et Rein V. Ulijn. « Cooperative Self-Assembly of Peptide Gelators and Proteins ». Biomacromolecules 14, no 12 (27 novembre 2013) : 4368–76. http://dx.doi.org/10.1021/bm401319c.

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Pengelly, Kate, Ana Loncar, Alex A. Perieteanu et John F. Dawson. « Cysteine engineering of actin self-assembly interfaces ». Biochemistry and Cell Biology 87, no 4 (août 2009) : 663–75. http://dx.doi.org/10.1139/o09-012.

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The Holmes model of filamentous actin (F-actin) and recent structural studies suggest specific atomic interactions between F-actin subunits. We tested these interactions through a cysteine-engineering approach with the goal of inhibiting filament formation by introducing chemical groups at sites important for polymerization. We substituted surface amino acids on the actin molecule with cysteine residues and tested the effect of producing these actin mutant proteins in a yeast expression system. The intrinsic folding and polymerization characteristics of the cysteine-engineered actin proteins were measured. The effect of chemical modification of the introduced cysteine residues on the polymerization of the actin mutant proteins was also examined. Modification of cysteine residues with large hydrophobic reagents resulted in polymerization inhibition. We examined the finding that the D288C actin protein does not polymerize under oxidizing conditions and forms protein aggregates when magnesium and EGTA are present. Chemical crosslinking experiments revealed the presence of a lower dimer when only D288C actin was present. When both D288C and A204C actin were present, crosslinking experiments support the proximity of Asp288 on the barbed end of one subunit to Ala204 on the pointed end of a neighboring subunit in the Holmes model of F-actin.
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Garcia-Seisdedos, Hector, Charly Empereur-Mot, Nadav Elad et Emmanuel D. Levy. « Proteins evolve on the edge of supramolecular self-assembly ». Nature 548, no 7666 (2 août 2017) : 244–47. http://dx.doi.org/10.1038/nature23320.

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Thèses sur le sujet "Proteins self-assembly"

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Edwards, Todd Criswell. « Self-assembly of proteins at interfaces and two-dimensional protein crystallization / ». Thesis, Connect to this title online ; UW restricted, 1999. http://hdl.handle.net/1773/8093.

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Wason, Akshita. « Investigation of lsm proteins as scaffolds in bionanotechnology ». Thesis, University of Canterbury. School of Biological Sciences, 2014. http://hdl.handle.net/10092/10065.

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Self-assembling materials have gained attention in the field of nanotechnology due to their potential to be used as building blocks for fabricating complex nanoscale devices. The biological world is abundant with examples of functional self-assembling biomolecules. Proteins are one such example, found in a variety of geometries and shapes. This research is focussed on the use of ring-shaped self-assembling proteins, called Lsm proteins, as componentary for applications in bionanotechnology. Lsm proteins were used because of their spontaneous association into stable rings, tolerance to mutations, and affinity to RNA. This thesis primarily focussed on the thermophilic Lsmα (from Methanobacterium. thermoautotrophicum) that assembles as heptameric rings. The oligomeric state of the heptameric protein, and hence the diameter of its central cavity, was manipulated by judiciously altering appropriate residues at the subunit interface. Lsmα presented a complex set of interactions at the interface. Out of the mutations introduced, R65P yielded a protein for which SEC and SAXS data were consistent with a hexameric state. Moreover, key residues, L70 and I71, were identified that contribute to the stability of the toroid structure. Covalent linking of rings provided nanotubular structures. To achieve this, the surface of the Lsmα ring scaffold was modified with Cys residues. This approach led to the formation of novel Lsmα nanotubes approximately 20 nm in length. Importantly, the assembly could be controlled by changing the redox conditions. As an alternative method to manipulate the supramolecular assembly, His6-tags were attached at the termini of the Lsmα sequence. The higher-order organisation of the constructs was influenced by the position of the His6-tag. The N-terminally attached His6-tag version of Lsmα showed a metal-dependent assembly into cage-like structures, approximately 9 nm across. This organisation was highly stable, reproducible, and reversible in nature. The results presented in this thesis aid the understanding of generating complex nanostructures via in vitro self-assembly. The Lsmα rings were assembled into higher-order architectures at the quaternary level by employing protein engineering strategies. Future work is necessary to functionalise these supramolecular structures; however, this study confirms the potential role of Lsmα proteins as a molecular building block in bionanotechnology.
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Santonicola, Mariagabriella. « Molecular self-assembly and interactions in solutions of membrane proteins and surfactants ». Access to citation, abstract and download form provided by ProQuest Information and Learning Company ; downloadable PDF file, 248 p, 2007. http://proquest.umi.com/pqdweb?did=1257806151&sid=6&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Thesis (Ph.D.)--University of Delaware, 2006.
Principal faculty advisors: Eric W. Kaler, College of Engineering; and Abraham M. Lenhoff, Dept. of Chemical Engineering. Includes bibliographical references.
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Mille, Christian. « Templating and self-assembly of biomimetic materials ». Doctoral thesis, Stockholms universitet, Institutionen för material- och miljökemi (MMK), 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-80459.

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This thesis focuses on the use of biomolecular assemblies for creating materials with novel properties. Several aspects of biomimetic materials have been investigated, from fundamental studies on membrane shaping molecules to the integration of biomolecules with inorganic materials. Triply periodic minimal surfaces (TPMS) are mathematically defined surfaces that partition space and present a large surface area in a confined space. These surfaces have analogues in many physical systems. The endoplasmic reticulum (ER) can form intricate structures and it acts as a replica for the wing scales of the butterfly C. rubi, which is characterized by electron microscopy and reflectometry. It was shown to contain a photonic crystal and an analogue to a TPMS. These photonic crystals have been replicated in silica and titania, leading to blue scales with replication on the nanometer scale. Replicas analyzed with left and right handed polarized light are shown be optically active. A macroporous hollow core particle was synthesized using a double templating method where a swollen block copolymer was utilized to create polyhedral nanofoam. Emulsified oil was used as a secondary template which gave hollow spheres with thin porous walls. The resulting material had a high porosity and low thermal conductivity. The areas of inorganic materials and functional biomolecules were combined to create a functional nanoporous endoskeleton. The membrane protein ATP synthase were incorporated in liposomes which were deposited on nanoporous silica spheres creating a tight and functional membrane. Using confocal microscopy, it was possible to follow the transport of Na+ through the membrane. Yop1p is a membrane protein responsible for shaping the ER. The protein was purified and reconstituted into liposomes of three different sizes. The vesicles in the 10-20 nm size range resulted in tubular structures. Thus, it was shown that Yop1p acts as a stabilizer of high curvature structures.

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 2: Manuscript. Paper 3: Submitted. Paper 4: Submitted. Paper 5: Submitted.

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Rodon, Fores Jennifer. « Localized protein-assisted self-assembly : from mechanism to applications ». Thesis, Strasbourg, 2019. http://www.theses.fr/2019STRAE017.

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La cellule est un système chimique complexe qui a bénéficié de milliards d’années d’évolution pour se perfectionner, et représente une machinerie très bien organisée ne laissant rien au hasard. Pour assurer son rôle, elle contrôle un ensemble de processus d’auto-assemblage où des composants isolés interagissent spontanément entre eux pour conduire à la formation de structures organisées et fonctionnelles telles que les microtubules, le collagène ou les fibres d’actine. En m’inspirant de l’organisation cellulaire, mon projet doctoral consiste en la conception de systèmes chimiques artificiels basés sur l’auto-assemblage de peptides originaux. Ces édifices donnent naissance à des hydrogels supramoléculaires d’intérêts dans le domaine des biomatériaux. Je m’intéresse à la fois à des aspect fondamentaux concernant la compréhension de l’initiation des processus d’auto-assemblage en présence de biomacromolécules, mais aussi à des problématiques plus appliquées consistant à élaborer des stratégies pour contrôler le lieu mais aussi le moment où ces édifices moléculaires auto-assemblés prennent naissance. Enfin, je m’intéresse à l’émergence des différentes propriétés apparaissant lors de la formation de certains auto-assemblages comme la catalyse ou l’auto-catalyse
The cell is a complex chemical system that has benefited from billions of years of evolution to perfect itself, and represents a very well organized machinery leaving nothing to chance. To ensure its role, it controls a set of self-assembly processes where isolated components interact spontaneously with each other to lead to the formation of organized and functional structures such as microtubules, collagen or actin fibers. Inspired by cellular organization, my doctoral project involves the design of artificial chemical systems based on the self-assembly of original peptides. These buildings give rise to supramolecular hydrogels of interest in the field of biomaterials. I am interested at the same time in fundamental aspects concerning the comprehension of the initiation of the processes of self-assembly in the presence of biomacromolecules, but also with more applied problems of elaborating strategies to control the place but also the moment where these self-assembled molecular structures originate. Finally, I am interested in the emergence of the different properties appearing during the formation of certain self-assemblies such as catalysis and auto-catalysis
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Skoda, Maximilian W. A. « Interaction of proteins with oligo(ethylene glycol) self-assembled monolayers ». Thesis, University of Oxford, 2007. http://ora.ox.ac.uk/objects/uuid:e36c47f8-1afc-4655-a84a-05bd06d0e45f.

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The aim of this thesis is the study of protein resistant oligo(ethylene glycol) (OEG) self-assembled monolayers (SAMs) using in situ techniques, such as neutron reflectivity (NR), polarisation modulation infrared spectroscopy (PMIR) and small-angle x-ray scattering (SAXS). In order to elucidate the mechanisms that lead to the nonfouling properties of these SAMs, the SAM-water, protein-protein and protein-SAM interactions have been studied separately. NR measurements, focused on the solid-liquid interface between OEG SAMs and water, show clear evidence of an extended layer with reduced density water. The reduction in density is up to 10% compared to the bulk value, and extends up to 5 nm into the bulk. The effective area (density reduction x length) of this reduced density water layer did not significantly change when the temperature was reduced to 5°C. In a complementary study, the interaction of water with protein-resistant HS(CHV2)11(OCH2CH2)3OMe monolayers was examined using in and ex situ PMIR. In particular, shifts in the position of the characteristic C-O-C stretching vibration were observed after the monolayers had been exposed to water. The shift in frequency increased when the SAM was observed in direct contact with a thin layer of water. It was found that the magnitude of the shift also depended on the surface coverage of the SAM. These results suggest a rather strong interaction of oligo(ethylene glycol) SAMs with water and indicate the penetration of water into the upper region of the monolayer. These findings indicate the presence of a tightly bound water layer at the SAM-water interface. Further NR studies of the interface between OEG SAMs and a highly concentrated protein solution revealed an oscillating protein density profile. A protein depleted region of about 4-5 nm close to the SAM was followed by a more densely populated region of 5-6 nm. These oscillations were then rapidly damped out until the bulk value was reached. The influence of temperature and salt concentration on the protein density profile was small, indicating a rather minor contribution of electrostatic interactions to the protein repulsive force. SAXS measurements of OEG coated gold colloids mixed with proteins in solution did also not show any pronounced salt concentration dependence of the colloid-protein interaction. The strong association of water with the SAM and the layer of tightly bound water, together with the lack of electrostatic repulsion, suggest that the adsorption of proteins is energetically hindered by the presence of a strongly bound hydration layer.
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Williamson, Alexander James. « Methods, rules and limits of successful self-assembly ». Thesis, University of Oxford, 2011. http://ora.ox.ac.uk/objects/uuid:9eb549f9-3372-4a38-9370-a9b0e58ca26b.

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The self-assembly of structured particles into monodisperse clusters is a challenge on the nano-, micro- and even macro-scale. While biological systems are able to self-assemble with comparative ease, many aspects of this self-assembly are not fully understood. In this thesis, we look at the strategies and rules that can be applied to encourage the formation of monodisperse clusters. Though much of the inspiration is biological in nature, the simulations use a simple minimal patchy particle model and are thus applicable to a wide range of systems. The topics that this thesis addresses include: Encapsulation: We show how clusters can be used to encapsulate objects and demonstrate that such `templates' can be used to control the assembly mechanisms and enhance the formation of more complex objects. Hierarchical self-assembly: We investigate the use of hierarchical mechanisms in enhancing the formation of clusters. We find that, while we are able to extend the ranges where we see successful assembly by using a hierarchical assembly pathway, it does not straightforwardly provide a route to enhance the complexity of structures that can be formed. Pore formation: We use our simple model to investigate a particular biological example, namely the self-assembly and formation of heptameric alpha-haemolysin pores, and show that pore insertion is key to rationalising experimental results on this system. Phase re-entrance: We look at the computation of equilibrium phase diagrams for self-assembling systems, particularly focusing on the possible presence of an unusual liquid-vapour phase re-entrance that has been suggested by dynamical simulations, using a variety of techniques.
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Wan, Fan. « Biomimetic Surface Coatings from Modular Amphiphilic Proteins ». Thesis, Université d'Ottawa / University of Ottawa, 2014. http://hdl.handle.net/10393/31639.

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Engineering of biofunctional scaffolds to precisely regulate cell behavior and tissue growth is of significance in regenerative medicine. Protein-based biomaterials are attractive candidates for functionalization of scaffold surfaces since the ability to precisely control protein sequence and structure allows for fine-tuning of cell-substrate interactions that regulate cell behavior. In this thesis, a series of de novo proteins for bio-functionalization of interfaces was designed, synthesized, and studied. These proteins are based on a diblock motif consisting of a surface-active, amphiphilic block β-sheet domain linked to a disordered, water-soluble block with a terminal functional domain. Several types of functional domains were investigated, including sequences that act as ligands for cell surface receptors and sequences that act as templates for the growth of inorganic particles. Under moderate temperature and pH conditions, the amphiphilic β-sheet block was shown to have a strong affinity to a variety of scaffold materials and to form stable protein coatings on hydrophobic materials by self-assembly. Moreover, the surface adsorption of the proteins was shown to have minimal impact on the presentation of the functional end domains in the soluble block. For the case of diblocks with the RGDS integrin binding sequence, the capability for mediating cell attachment and spreading was demonstrated via control over ligand density on hydrophobic polymer surfaces. The case of diblock proteins with templating domains for inorganic materials was investigated for two systems. First, hydroxyapatite-binding domains were ligated to the end terminus of the water-soluble block to develop proteins for possible bone regeneration applications. It was demonstrated that the hydroxyapatite-binding domain had strong affinity to hydroxyapatite nanoparticles and was able to induce calcium phosphate mineralization on the surfaces coated with diblock proteins from dilute solutions with Ca2+.and PO43-. Next, a silver-binding domain was ligated to the end terminus to create a diblock protein for potential antimicrobial surface applications. The silver-binding domain was shown to accumulate and reduce silver ions, resulting in the formation of silver nanoparticles on the surfaces functionalized by the protein.
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Kurland, Nicholas. « Design of Engineered Biomaterial Architectures Through Natural Silk Proteins ». VCU Scholars Compass, 2013. http://scholarscompass.vcu.edu/etd/571.

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Silk proteins have provided a source of unique and versatile building blocks in the fabrication of biomedical devices for addressing a range of applications. Critical to advancing this field is the ability to establish an understanding of these proteins in their native and engineered states as well as in developing scalable processing strategies, which can fully exploit or enhance the stability, structure, and functionality of the two constituent proteins, silk fibroin and sericin. The research outlined in this dissertation focuses on the evolution in architecture and capability of silks, to effectively position a functionally-diverse, renewable class of silk materials within the rapidly expanding field of smart biomaterials. Study of the process of building macroscopic silk fibers provides insight into the initial steps in the broader picture of silk assembly, yielding biomaterials with greatly improved attributes in the assembled state over those of protein precursors alone. Self-organization processes in silk proteins enable their aggregation into highly organized architectures through simple, physical association processes. In this work, a model is developed for the process of aqueous behavior and aggregation, and subsequent two-dimensional behavior of natural silk sericin, to enable formation of a range of distinct, complex architectures. This model is then translated to an engineered system of fibroin microparticles, demonstrating the role of similar phenomena in creating autonomously-organized structures, providing key insight into future “bottom up” assembly strategies. The aqueous behavior of the water-soluble silk sericin protein was then exploited to create biocomposites capable of enhanced response and biocompatibility, through a novel protein-template strategy. In this work, sericin was added to the biocompatible and biodegradable poly(amino acid), poly(aspartic acid), to improve its pH-dependent swelling response. This work demonstrated the production of a range of porous scaffolds capable providing meaningful response to environmental stimuli, with application in tissue engineering scaffolds and biosensing technologies. Finally, to expand the capabilities of silk proteins beyond process-driven parameters to directly fabricate engineered architectures, a method for silk photopatterning was explored, enabling the direct fabrication of biologically-relevant structures at the micro and nanoscales. Using a facile bioconjugation strategy, native silk proteins could be transformed into proteins with a photoactive capacity. The well-established platform of photolithography could then be incorporated into fabrication strategies to produce a range of architectures capable of addressing spatially-directed material requirements in cell culture and further applications in the use of non-toxic, renewable biological materials.
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Valkov, Eugene. « Design and analysis of self-assembling protein systems ». Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.670100.

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Livres sur le sujet "Proteins self-assembly"

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McManus, Jennifer J., dir. Protein Self-Assembly. New York, NY : Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9678-0.

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Vasconcelos, Andreia. Protein matrices for wound dressings : Self-assembly of fibrous proteins into new materials. LAP Lambert Academic Publishing, 2011.

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(Editor), A. Aggeli, N. Boden (Editor) et Zhang Shuguang (Editor), dir. Self-Assembling Peptide Systems in Biology, Medicine and Engineering. Springer, 2001.

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Carter, Joshua D., Chenxiang Lin, Yan Liu, Hao Yan et Thomas H. LaBean. DNA-based self-assembly of nanostructures. Sous la direction de A. V. Narlikar et Y. Y. Fu. Oxford University Press, 2017. http://dx.doi.org/10.1093/oxfordhb/9780199533053.013.24.

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This article examines the DNA-based self-assembly of nanostructures. It first reviews the development of DNA self-assembly and DNA-directed assembly, focusing on the main strategies and building blocks available in the modern molecular construction toolbox, including the design, construction, and analysis of nanostructures composed entirely of synthetic DNA, as well as origami nanostructures formed from a mixture of synthetic and biological DNA. In particular, it considers the stepwise covalent synthesis of DNA nanomaterials, unmediated assembly of DNA nanomaterials, hierarchical assembly, nucleated assembly, and algorithmic assembly. It then discusses DNA-directed assembly of heteromaterials such as proteins and peptides, gold nanoparticles, and multicomponent nanostructures. It also describes the use of complementary DNA cohesion as 'smart glue' for bringing together covalently linked functional groups, biomolecules, and nanomaterials. Finally, it evaluates the potential future of DNA-based self-assembly for nanoscale manufacturing for applications in medicine, electronics, photonics, and materials science.
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McManus, Jennifer J. Protein Self-Assembly : Methods and Protocols. Springer New York, 2020.

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McManus, Jennifer J. Protein Self-Assembly : Methods and Protocols. Springer New York, 2019.

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Bitan, Gal, Sandra Macedo-Ribeiro et Maria Rosário Almeida, dir. Strategies and Tools for Modulating Pathologic Protein Self-Assembly in Proteinopathies. Frontiers Media SA, 2022. http://dx.doi.org/10.3389/978-2-88976-711-3.

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Sherwood, Dennis, et Paul Dalby. Thermodynamics today – and tomorrow. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.003.0026.

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This last chapter explores the frontiers of how thermodynamics is currently being applied to biology, moving from the scale of the molecule to the scale of the cell. The key theme is ‘self-assembly’ – the process by which macromolecules spontaneously assemble into larger structures such as cell membranes, cell organelles, cells, and ultimately organisms. The starting point is the simplest process of self-assembly, the formation of a liquid from the condensation of a gas, which draws on some results from Chapter 15, and develops the concept of nucleation, this leads to a discussion of protein aggregation, and how virus particles are formed. The chapter, and the book, ends with a key challenge for the future: how can we deliberately design self-assembling systems that can perform valuable functions?
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Narlikar, A. V., et Y. Y. Fu, dir. Oxford Handbook of Nanoscience and Technology. Oxford University Press, 2017. http://dx.doi.org/10.1093/oxfordhb/9780199533060.001.0001.

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This volume highlights engineering and related developments in the field of nanoscience and technology, with a focus on frontal application areas like silicon nanotechnologies, spintronics, quantum dots, carbon nanotubes, and protein-based devices as well as various biomolecular, clinical and medical applications. Topics include: the role of computational sciences in Si nanotechnologies and devices; few-electron quantum-dot spintronics; spintronics with metallic nanowires; Si/SiGe heterostructures in nanoelectronics; nanoionics and its device applications; and molecular electronics based on self-assembled monolayers. The volume also explores the self-assembly strategy of nanomanufacturing of hybrid devices; templated carbon nanotubes and the use of their cavities for nanomaterial synthesis; nanocatalysis; bifunctional nanomaterials for the imaging and treatment of cancer; protein-based nanodevices; bioconjugated quantum dots for tumor molecular imaging and profiling; modulation design of plasmonics for diagnostic and drug screening; theory of hydrogen storage in nanoscale materials; nanolithography using molecular films and processing; and laser applications in nanotechnology. The volume concludes with an analysis of the various risks that arise when using nanomaterials.
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Narlikar, A. V., et Y. Y. Fu, dir. Oxford Handbook of Nanoscience and Technology. Oxford University Press, 2017. http://dx.doi.org/10.1093/oxfordhb/9780199533053.001.0001.

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This Handbook presents important developments in the field of nanoscience and technology, focusing on the advances made with a host of nanomaterials including DNA and protein-based nanostructures. Topics include: optical properties of carbon nanotubes and nanographene; defects and disorder in carbon nanotubes; roles of shape and space in electronic properties of carbon nanomaterials; size-dependent phase transitions and phase reversal at the nanoscale; scanning transmission electron microscopy of nanostructures; the use of microspectroscopy to discriminate nanomolecular cellular alterations in biomedical research; holographic laser processing for three-dimensional photonic lattices; and nanoanalysis of materials using near-field Raman spectroscopy. The volume also explores new phenomena in the nanospace of single-wall carbon nanotubes; ZnO wide-bandgap semiconductor nanostructures; selective self-assembly of semi-metal straight and branched nanorods on inert substrates; nanostructured crystals and nanocrystalline zeolites; unusual properties of nanoscale ferroelectrics; structural, electronic, magnetic, and transport properties of carbon-fullerene-based polymers; fabrication and characterization of magnetic nanowires; and properties and potential of protein-DNA conjugates for analytic applications.
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Chapitres de livres sur le sujet "Proteins self-assembly"

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Ueno, Takafumi. « Coordination Chemistry in Self-Assembly Proteins ». Dans SpringerBriefs in Molecular Science, 61–68. Tokyo : Springer Japan, 2013. http://dx.doi.org/10.1007/978-4-431-54370-1_7.

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Safinya, Cyrus R., et Yi Shen. « Membrane-Associated-Proteins : Self-Assembly, Interactions, and Biomolecular Materials ». Dans Physics of Biomaterials : Fluctuations, Selfassembly and Evolution, 103–34. Dordrecht : Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-1722-4_4.

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Varga, Melinda, et Nuriye Korkmaz. « S-Layer Proteins as Self-Assembly Tool in Nano Bio Technology ». Dans Bio and Nano Packaging Techniques for Electron Devices, 419–26. Berlin, Heidelberg : Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-28522-6_20.

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Ford, Marijn G. J., et Rajesh Ramachandran. « Light Scattering Techniques to Assess Self-Assembly and Hydrodynamics of Membrane Trafficking Proteins ». Dans Membrane Trafficking, 259–84. New York, NY : Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2209-4_18.

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Malik, Ravinder, Jing Di, Gayatri Nair, Aida Attar, Karen Taylor, Edmond Teng, Frank-Gerrit Klärner, Thomas Schrader et Gal Bitan. « Using Molecular Tweezers to Remodel Abnormal Protein Self-Assembly and Inhibit the Toxicity of Amyloidogenic Proteins ». Dans Methods in Molecular Biology, 369–86. New York, NY : Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7811-3_24.

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Leon, Lorraine, et Matthew Tirrell. « Protein Analogous Micelles ». Dans Self-Assembly, 179–205. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2018. http://dx.doi.org/10.1002/9781119001379.ch6.

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Dong, Xuehui, Aaron Huang, Allie Obermeyer et Bradley D. Olsen. « Self-Assembly of Protein−Polymer Conjugates ». Dans Self-Assembly, 207–55. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2018. http://dx.doi.org/10.1002/9781119001379.ch7.

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Qiao, Shanpeng, et Junqiu Liu. « Protein Self-Assembly : Strategies and Applications ». Dans Handbook of Macrocyclic Supramolecular Assembly, 915–55. Singapore : Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-2686-2_38.

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Qiao, Shanpeng, et Junqiu Liu. « Protein Self-Assembly : Strategies and Applications ». Dans Handbook of Macrocyclic Supramolecular Assembly, 1–41. Singapore : Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-1744-6_38-1.

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Chakraborti, Soumyananda, Antti Korpi, Jonathan G. Heddle et Mauri A. Kostiainen. « Electrostatic Self-Assembly of Protein Cage Arrays ». Dans Methods in Molecular Biology, 123–33. New York, NY : Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0928-6_8.

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Actes de conférences sur le sujet "Proteins self-assembly"

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MIRNY, LEONID. « THE PROTEIN-FOLDING NUCLEUS : FROM SIMPLE MODELS TO REAL PROTEINS ». Dans Folding and Self-Assembly of Biological Macromolecules Conference. WORLD SCIENTIFIC, 2004. http://dx.doi.org/10.1142/9789812703057_0011.

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Layton, Bradley E. « Self-Assembly Limits in Structural Proteins ». Dans ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46019.

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A mechanics-based model is presented which predicts a “neutral annulus” for quasi-crystalline self-assembling nanostructure such as collagen fibrils, wherein transcript length, torsional and axial stiffness along with primary and quaternary protein structure limit the size to which these structures may aggregate. In the present treatment, a neutral annulus is predicted at 0.625 of the fibril radius, wherein portions of the fibril interior to the neutral annulus are in compression, balanced by portions exterior to the neutral annulus which are in tension.
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Cao, Yiping, et Mahesh Khot. « Food protein self-assembly towards high-performance functional materials ». Dans 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/oyxx3948.

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Proteins not only determine the essential life activities of living organisms and the nutritional value of food products, but also are promising raw materials for designing functional materials, including in the fields of food science, environmental science, and nanomaterials. In the last decade, self-assembly of food proteins, particularly fibrillization, has attracted significant interest, as the assembled nanostructures are characterized by abundant b-sheet structures, large aspect ratio, and diverse surface functional groups. These features offer the possibility to overcome existing technological bottlenecks, and the rational utilization can yield high-performance materials. This talk will focus on two examples: protein gels and plastics. In the first example, a quantitative relationship was established between the microstructure of protein nanofibrils and the macroscopic mechanical properties of the resulting gels. This was successfully used to build protein gels with mechanical properties comparable to those of artificial meat. In the second example, protein-based plastics with high mechanical property and reduced hygroscopicity are developed by combining protein copolymerization and self-assembly. This provides a potential strategy for developing sustainable food packaging materials.
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BENNER, STEVEN. « EVOLUTION-BASED GENOME ANALYSIS : AN ALTERNATIVE TO ANALYZE FOLDING AND FUNCTION IN PROTEINS ». Dans Folding and Self-Assembly of Biological Macromolecules Conference. WORLD SCIENTIFIC, 2004. http://dx.doi.org/10.1142/9789812703057_0001.

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Athamneh, Ahmad, et Justin Barone. « Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins ». Dans ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-540.

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Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.
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Dee, Derek, Fan Bu, Lanfang Shi et Sara Zamani. « Comparing the structure and functionality of amyloid fibrils assembled from peanut, pea, lentil, and mung bean proteins ». Dans 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/kkyn7687.

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Protein structure dictates functionality, and one way to dramatically alter protein structure is to induce proteins to self-assemble into amyloid fibrils. Amyloid fibrils, or nanofibrils, are long (100–1000’s nm), narrow (10’s nm), highly-organized protein aggregates that hold promise for various applications in biotechnology and food. Converting plant proteins into fibrils may improve their functionality and create sustainable materials, yet most nanofibril research has focused on animal-derived proteins, so there is a need to learn more about fibrils derived from plant proteins. This project compared fibrils assembled from crude protein extracts from peanut, pea, lentils and mung bean, comparing their fibril assembly kinetics, fibril structure, emulsification and viscosity properties. Peanut and mung bean fibrils assembled much faster (kPeanut = 0.90 ± 0.40 h-1, kMungbean = 0.95 ± 0.40 h-1) compared to pea and lentil fibrils (kPea = 0.19 ± 0.03 h-1, kLentil = 0.24 ± 0.01 h-1), at 80 °C, pH 2 with stirring. Fibrils from the different legume proteins displayed markedly different structures that could be generally classified as either long and straight (1000’s nm) or short and curly (100’s nm). The former are more similar to fibrils typically generated from animal proteins (e.g., whey, egg white proteins) while the latter are typical of legume protein fibrils presented in the literature. The longer/straighter or shorter/curly fibrils displayed unique functionalities (emulsion particle size and viscosity profiles) that did not directly correlate with fibril morphology, although several confounding factors limit the establishment of direct structure-function associations. This work indicates several approaches to optimize the assembly of legume protein fibrils that may find use in new plant-based materials and foods.
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Verma, Gunjan, Sipra Choudhury, P. A. Hassan, Dinesh K. Aswal et Anil K. Debnath. « Fabrication Of Nano-Silver Thin Films Using Self Assembly And Its Interaction With Proteins ». Dans INTERNATIONAL CONFERENCE ON PHYSICS OF EMERGING FUNCTIONAL MATERIALS (PEFM-2010). AIP, 2010. http://dx.doi.org/10.1063/1.3530543.

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Creasy, M. Austin, et Donald J. Leo. « Modeling Bilayer Systems as Electrical Networks ». Dans ASME 2010 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2010. http://dx.doi.org/10.1115/smasis2010-3791.

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Bilayers are synthetically made cell membranes that are used to study cell membrane properties or make functional devices that use the properties of the cell membrane components. Lipids and proteins are two of the main components of a cell membrane. Lipids are amphiphilic molecules that can self assemble into organized structures in the presences of water and this self assembly property can be used to form bilayers. Because of the amphiphilic nature of the lipids, a bilayer is impermeable to ion flow. Proteins are the active structures of a cell membrane that opens pores through the membrane for ions and other molecules to pass. Proteins are made from amino acids and have varying properties that depend on its configuration. Some proteins are activated by reactions (chemical, thermal, etc) or gradients induced across the bilayer. One way of testing bilayers to find bilayer properties is to induce a potential gradient across a membrane that induces ion flow and this flow can be measured as an electrical current. But, these pores may be voltage gated or activated by some other stimuli and therefore cannot be modeled as a linear conductor. Usually the conductance of the protein is a nonlinear function of the input that activates the protein. A small system that consists of a single bilayer and protein with few changing components can be easily modeled, but as systems become larger with multiple bilayers, multiple variables, and multiple proteins, the models will become more complex. This paper looks at how to model a system of multiple bilayers and the peptide alamethicin. An analytical expression for this peptide is used to match experimental data and a short study on the sensitivity of the variables is performed.
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Takshi, Arash, Fatemeh Khorramshahi, Houman Yaghoubi, Daniel Jun et J. Thomas Beatty. « Ion-sensitive field-effect transistors with Si3N4 and TaO2 gate insulator for studying self-assembly of photosynthetic proteins ». Dans Organic and Hybrid Sensors and Bioelectronics XII, sous la direction de Ruth Shinar, Ioannis Kymissis et Emil J. List-Kratochvil. SPIE, 2019. http://dx.doi.org/10.1117/12.2527358.

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Puskar, Kathleen, Leonard Apeltsin, Shlomo Ta’asan, Russell Schwartz et Philip R. LeDuc. « Bridging Mechanical Stimulation of Cellular and Molecular Structure Through Lattice Based Computational Simulations ». Dans ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-61613.

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Understanding the connection between mechanics and cell structure requires a critical exploration of molecular structure. One of these molecular bridges is known to be the cytoskeleton, which is involved with intracellular organization and mechanotransduction. In order to examine the structure in cells, we have developed a computational simulation that is able to probe the self-assembly of actin filaments through a lattice based Monte Carlo method. We have modeled the polymerization of these filaments based upon the interactions of globular actin through a probabilistic scheme with both inert and active proteins. The results show similar response to classic ordinary differential equations at low molecular concentrations, but a bi-phasic divergence at realistic concentrations for living mammalian cells. Further, these inert monomers have a limiting effect based upon their relative density ratios, which alter the polymerization process. Finally, by introducing localized mobility parameters, we are able to set up molecular gradients that are found in non-homogeneous protein distributions in vitro. This method and results have potential applications in cell and molecular biology as well as self assembly in inorganic systems.
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