Relevant bibliographies by topics / Beta barrel membrane proteins

Academic literature on the topic 'Beta barrel membrane proteins'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Beta barrel membrane proteins"

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Solan, Ron, Joana Pereira, Andrei N. Lupas, Rachel Kolodny, and Nir Ben-Tal. "Gram-negative outer-membrane proteins with multiple β-barrel domains." Proceedings of the National Academy of Sciences 118, no. 31 (July 30, 2021): e2104059118. http://dx.doi.org/10.1073/pnas.2104059118.

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Outer-membrane beta barrels (OMBBs) are found in the outer membrane of gram-negative bacteria and eukaryotic organelles. OMBBs fold as antiparallel β-sheets that close onto themselves, forming pores that traverse the membrane. Currently known structures include only one barrel, of 8 to 36 strands, per chain. The lack of multi-OMBB chains is surprising, as most OMBBs form oligomers, and some function only in this state. Using a combination of sensitive sequence comparison methods and coevolutionary analysis tools, we identify many proteins combining multiple beta barrels within a single chain; combinations that include eight-stranded barrels prevail. These multibarrels seem to be the result of independent, lineage-specific fusion and amplification events. The absence of multibarrels that are universally conserved in bacteria with an outer membrane, coupled with their frequent de novo genesis, suggests that their functions are not essential but rather beneficial in specific environments. Adjacent barrels of complementary function within the same chain may allow for functions beyond those of the individual barrels.
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Miles, A. J., and B. A. Wallace. "Circular dichroism spectroscopy of membrane proteins." Chemical Society Reviews 45, no. 18 (2016): 4859–72. http://dx.doi.org/10.1039/c5cs00084j.

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Noinaj, Nicholas, Adam Kuszak, Curtis Balusek, JC Gumbart, Petra Lukacik, Hoshing Chang, Nicole Easley, Trevor Lithgow, and Susan Buchanan. "The role of BamA in the biogenesis of beta-barrel membrane proteins." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C578. http://dx.doi.org/10.1107/s2053273314094212.

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Beta-barrel membrane proteins are essential for nutrient import, signaling, motility, and survival. In Gram-negative bacteria, the beta-barrel assembly machinery (BAM) complex is responsible for the biogenesis of beta-barrel outer membrane proteins (OMPs), with homologous complexes found in mitochondria and chloroplasts. Despite their essential roles, exactly how these OMPs are formed remains unknown. The BAM complex consists of a central and essential component called BamA (an OMP itself) and four lipoproteins called BamB-E. While the structure of the lipoproteins have been reported, the structure of full length BamA has been elusive. Recently though, we described the structure of BamA from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi. BamA consists of a large periplasmic domain attached to a 16-strand transmembrane beta-barrel domain. Together, our crystal structures and molecule dynamics (MD) simulations revealed several structural features which gave clues to the mechanism by which BamA catalyzes beta-barrel assembly. The first is that the interior cavity is accessible in one BamA structure and conformationally closed in the other. Second, an exterior rim of the beta-barrel has a distinctly narrowed hydrophobic surface, locally destabilizing the outer membrane. Third, the beta-barrel can undergo lateral opening, suggesting a route from the interior cavity in BamA into the outer membrane. And fourth, a surface exposed exit pore positioned above the lateral opening site which may play a role in the biogenesis of extracellular loops. In this presentation, the crystal structures and MD simulations of BamA will be presented along with our work looking at the role of these four structural features in the role of BamA within the BAM complex.
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Tian, Wei, Hammad Naveed, and Jie Liang. "Improving 3D Structure Prediction of Beta-Barrel Membrane Proteins." Biophysical Journal 112, no. 3 (February 2017): 55a. http://dx.doi.org/10.1016/j.bpj.2016.11.333.

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Lessen, Henry J., Patrick Fleming, Karen G. Fleming, and Alexander J. Sodt. "Transmembrane Beta-Barrel Proteins Rigidify the Bacterial Outer Membrane." Biophysical Journal 116, no. 3 (February 2019): 327a. http://dx.doi.org/10.1016/j.bpj.2018.11.1774.

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Roterman, Irena, Katarzyna Stapor, Piotr Fabian, and Leszek Konieczny. "The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins." Membranes 11, no. 8 (July 30, 2021): 580. http://dx.doi.org/10.3390/membranes11080580.

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β-barrel membrane proteins have several important biological functions, including transporting water and solutes across the membrane. They are active in the highly hydrophobic environment of the lipid membrane, as opposed to soluble proteins, which function in a more polar, aqueous environment. Globular soluble proteins typically have a hydrophobic core and a polar surface that interacts favorably with water. In the fuzzy oil drop (FOD) model, this distribution is represented by the 3D Gauss function (3DG). In contrast, membrane proteins expose hydrophobic residues on the surface, and, in the case of ion channels, the polar residues face inwards towards a central pore. The distribution of hydrophobic residues in membrane proteins can be characterized by means of 1–3DG, a complementary 3D Gauss function. Such an analysis was carried out on the transmembrane proteins of bacteria, which, despite the considerable similarities of their super-secondary structure (β-barrel), have highly differentiated properties in terms of stabilization based on hydrophobic interactions. The biological activity and substrate specificity of these proteins are determined by the distribution of the polar and nonpolar amino acids. The present analysis allowed us to compare the ways in which the different proteins interact with antibiotics and helped us understand their relative importance in the development of the resistance mechanism. We showed that beta barrel membrane proteins with a hydrophobic core interact less strongly with the molecules they transport.
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Kazemian, Hassan B., and Cedric Maxime Grimaldi. "Cascading classifier application for topology prediction of transmembrane beta-barrel proteins." Journal of Bioinformatics and Computational Biology 18, no. 06 (October 15, 2020): 2050034. http://dx.doi.org/10.1142/s0219720020500341.

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Membrane proteins are a major focus for new drug discovery. Transmembrane beta-barrel (TMB) proteins play key roles in the translocation machinery, pore formation, membrane anchoring and ion exchange. Given their key roles and the difficulty in membrane protein structure determination, the use of computational modeling is essential. This paper focuses on the topology prediction of TMB proteins. In the field of bioinformatics, many years of research has been spent on the topology prediction of transmembrane alpha-helices. The efforts to TMB proteins topology prediction have been overshadowed and the prediction accuracy could be improved with further research. Various methodologies have been developed in the past for the prediction of TMB protein topology, however, the use of cascading classifier has never been fully explored. This research presents a novel approach to TMB topology prediction with the use of a cascading classifier. The MATLAB computer simulation results show that the proposed methodology predicts TMB proteins topologies with high accuracy for randomly selected proteins. By using the cascading classifier approach, the best overall accuracy is 76.3% with a precision of 0.831 and recall or probability of detection of 0.799 for TMB topology prediction. The accuracy of 76.3% is achieved using a two-layers cascading classifier.
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Jain, Sumita, and Marcia B. Goldberg. "Requirement for YaeT in the Outer Membrane Assembly of Autotransporter Proteins." Journal of Bacteriology 189, no. 14 (May 18, 2007): 5393–98. http://dx.doi.org/10.1128/jb.00228-07.

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ABSTRACT Autotransporters constitute the largest group of secreted proteins in gram-negative bacteria. Autotransporter secretion involves the insertion of a carboxy-terminal beta barrel into and the translocation of an amino-terminal domain across the outer membrane. Here, we demonstrate that secretion of autotransporters from several organisms requires the outer membrane assembly factor YaeT.
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Naveed, Hammad, and Jie Liang. "Weakly Stable Regions and Protein-Protein Interactions in Beta-Barrel Membrane Proteins." Current Pharmaceutical Design 20, no. 8 (March 31, 2014): 1268–73. http://dx.doi.org/10.2174/13816128113199990071.

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Columbus, Linda, Daniel A. Fox, and Ryan H. Lo. "Strategies for the Solution NMR Structure Determination of Beta-Barrel Membrane Proteins." Biophysical Journal 102, no. 3 (January 2012): 422a—423a. http://dx.doi.org/10.1016/j.bpj.2011.11.2311.

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Dissertations / Theses on the topic "Beta barrel membrane proteins"

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Arjara, Gitrada Rees Douglas C. Gray Harry B. Richards John. "Refolding a beta-barrel membrane protein /." Diss., Pasadena, Calif. : California Institute of Technology, 2007. http://resolver.caltech.edu/CaltechETD:etd-05292007-061922.

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Pocanschi, Cosmin Lorin. "Folding and stability of beta-barrel membrane proteins from Gram-negative bacteria." [S.l. : s.n.], 2005. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-16869.

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Klein, Astrid. "A structural analysis of the TOB complex, the insertase for Beta-barrel proteins of the mitochondrial outer membrane." Diss., lmu, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-150786.

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Klein, Astrid [Verfasser], and Angelika [Akademischer Betreuer] Böttger. "A structural analysis of the TOB complex, the insertase for beta-barrel proteins of the mitochondrial outer membrane / Astrid Klein. Betreuer: Angelika Böttger." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2011. http://d-nb.info/1028490461/34.

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Miles, Jr George Emmett. "On the structure and assembly of staphylococcal leukocidin: a study of the molecular architecture of beta-barrel pore-forming toxins." Texas A&M University, 2003. http://hdl.handle.net/1969.1/3952.

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Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of β-barrel pore-forming toxins (β-PFTs). By contrast, other β-PFTs form homooligomeric pores. For example, the staphylococcal α- hemolysin is a homoheptamer. Limited and controversial data exist on the assembly and molecular architecture of the leukocidin pore. In this work, biochemical and biophysical methods were used to characterize the leukocidin pore produced by the LukF (HlgB) and LukS (HlgC) components encoded by Staphylococcus aureus. I demonstrate that LukF and LukS assemble to form an SDS-stable pore on rabbit erythrocyte membranes. In addition, the pore-forming properties of recombinant leukocidin were investigated with planar lipid bilayers. Although leukocidins and staphylococcal α-hemolysin share partial sequence identity and related folds, LukF and LukS produce a pore with a unitary conductance of 2.5 nS (1 M KCl, 5 mM HEPES, pH 7.4), which is over three times greater than that of α-hemolysin measured under the same conditions. The subunit composition and stoichiometry of a leukocidin pore were determined by two independent methods, gel shift electrophoresis and sitespecific chemical modification during single channel recording. Four LukF and four LukS subunits were shown to co-assemble into an octameric transmembrane structure. The existence of an additional subunit in part explains properties of the leukocidin pore, such as its high conductance. Additionally, this is the first time that either technique has been applied successfully to assess the composition of a heteromeric membrane protein. It is also relevant to understanding the mechanism of assembly of β-PFT pores, and suggests new possibilities for engineering these proteins. In additional studies, the HlyII pore encoded by Bacillus cereus was found to form a homoheptameric transmembrane pore with properties conforming in general with those of other members of the class of β-PFTs. HlyII possesses additional properties which make it an attractive candidate for applications in biotechnology, such as an oligomer with a high thermal stability in the presence of SDS and the ability of the pore to remain open at high transmembrane potentials.
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Jorgenson, Matthew Allan. "A tale of two RLPAs : studies of cell division in Escherichia coli and Pseudomonas aeruginosa." Diss., University of Iowa, 2014. https://ir.uiowa.edu/etd/1342.

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Rare lipoprotein A (RlpA) has been studied previously only in Escherichia coli, where it localizes to the septal ring and scattered foci along the lateral wall, but mutants have no phenotypic change. In this thesis, we show rlpA mutants of Pseudomonas aeruginosa form chains of short, fat cells when grown in media of low osmotic strength. These morphological defects indicate RlpA is needed for efficient separation of daughter cells and maintenance of rod shape. Analysis of peptidoglycan sacculi from a ΔrlpA mutant revealed increased tetra and hexasaccharides that lack stem peptides (hereafter called "naked glycans"). Incubation of these sacculi with purified RlpA resulted in release of naked glycans containing 1,6-anhydro N-acetylmuramic acid ends. RlpA did not degrade sacculi from wild-type cells unless the sacculi were subjected to a limited digestion with an amidase to remove some of the stem peptides. Collectively, these findings indicate RlpA is a lytic transglycosylase with a strong preference for naked glycan strands. We propose that RlpA activity is regulated in vivo by substrate availability, and that amidases and RlpA work in tandem to degrade peptidoglycan in the division septum and lateral wall. Our discovery that RlpA from P. aeruginosa is a lytic transglycosylase motivated us to reinvestigate RlpA from E. coli. We confirmed predictions that RlpA of E. coli is an outer membrane protein and determined its abundance to be about 600 molecules per cell. However, multiple efforts to demonstrate that E. coli RlpA is a lytic transglycosylase were unsuccessful and the function of this protein in E. coli remains obscure.
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Garrow, Andrew Gordon. "Search algorithms for transmembrane beta-barrel proteins." Thesis, University of Leeds, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.427773.

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Pongprayoon, Prapasiri. "Molecular modelling of β-barrel outer membrane proteins." Thesis, University of Oxford, 2010. http://ora.ox.ac.uk/objects/uuid:0ed0c22f-027e-4be1-a64c-0819888bbebc.

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In Gram-negative bacteria, the Outer membrane (OM) acts as a first barrier to screen unwanted compounds whilst enabling ions and very small solutes to diffuse into the cell. Most of nutrients and essential ions are effectively transported across a membrane via the outer membrane proteins (OMPs). The water-filled β- barrel OMPs are called porins. These pores are classified into two groups, non- specific and substrate-specific porins. Each of them has different mechanisms to facilitate its substrate translocation. To reveal the process of substrate permeation and selectivity in microscopic detail, molecular dynamics (MD) simulations and applications were performed in this thesis. The studies in this thesis focus on a series of classical porins. These proteins share similar feature where extracellular loop(s) (generally loop 3 (L3)) is folded into the middle of the pore and act as a constriction site which is important for substrate specificity and selectivity. The studies firstly concentrate on the structural properties and dynamics of the general trimeric porins, OmpC and OmpF whose sequences share 60% identity. OmpC and OmpF are found to have similar mechanism of latching loop (L2) to maintain trimeric stability. The smaller pore size allows OmpC to be more cation-selective than OmpF. Additionally, the major driving force for cation permeation in both porins is not from electrostatic properties. This differs from the phosphate-selective porin, trimeric OprP, where a phosphate diffusion depends on electrostatic interactions with positively charged pore-lining residues. The charge brush-like behavior of interior Arg and Lys residues plays a major role in phosphate selectivity. Also, the free energy profiles (PMF) reveal two key regions that are important for differentiating phosphate from other anions. The brush-like mechanism of OprP were also implanted to the simplified model pores in order to determine the possibility of transferring phosphate-selective properties of OprP to a model which may be useful for future design of nanopores. It is found that the duplication of functional residues and pore cavity can turn a model into the highly phosphate-selective pore. Importantly, the phosphate-binding affinity is dependent on the ability of the pore to interfere and occupy the hydration shell of a translocating phosphate where such ability can be maximized by an increase in sidechain flexibility. In case of uptake of more complex substrates, OpdK also employs a constriction site to select its substrate, aromatic vanillate (VNL) with total charge of -1. Unlike ion-specific porins, the free VNL is attracted by polar and aromatic interactions and sequentially directed through the periplasmic vestibule by charged residues insides the pore. The correct orientation of VNL on arrival is crucial for OpdK to recognize and enable the permeation process.
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Schiller, Stina. "Evolutive In-vitro-Adaption eines thermostabilen ([beta][alpha]8-barrel-Proteins [beta-alpha-8-barrel-Proteins] an die Katalyse einer abiotischen Reaktion." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=970732600.

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Tran, Thuong Van Du. "Modeling and predicting super-secondary structures of transmembrane beta-barrel proteins." Phd thesis, Ecole Polytechnique X, 2011. http://tel.archives-ouvertes.fr/tel-00647947.

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Les protéines transmembranaires canaux-β (TMBs) se trouvent dans les membranes externes des bactéries à Gram négatif, des mitochondries ainsi que des chloroplastes. Elles traversent entièrement la membrane cellulaire et exercent différentes fonctions importantes. Vu qu'il y a un petit nombre des structures des TMBs déterminées, en raison des difficultés avec les méthodes expérimentales, il est douteux que ces approches puis- sent bien trouver et prédire les TMBs qui ne sont pas homologues avec celles connues. Nous construisons un modèle de graphe pour la classification et la prédiction de structures super-secondaires permutées des TMBs à partir de leur séquence d'acides aminés, en se basant sur la minimisation d'énergie. Le modèle ne dépend essentiellement pas de l'apprentissage. Les algorithmes sont rapides, robustes avec des performances com- parables à celles des meilleures méthodes actuelles qui utilisent l'apprentissage. Cette méthode peut être donc utile pour le screening des génomes. Outre la performance de prédiction et de classification, cette étude donne une vue plus profonde de la structure des TMBs en tenant compte des contraintes physicochimiques des membranes biologiques. Les structures permutées prédites peuvent aussi aider à mieux comprendre le mécanisme du repliement des TMBs.
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Books on the topic "Beta barrel membrane proteins"

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Brazil, Derek P. Regulation of phospholipase C-[beta]2 by G protein [beta] [gamma] subunits. Dublin: University College Dublin, 1996.

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M, Hooper N., ed. Alzheimer's disease: Methods and protocols. Totowa, N.J: Humana Press, 2000.

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McGeer, Patrick L., Chikako Tanaka, and Yasuo Ihara. Neuroscientific Basis of Dementia. Springer Basel AG, 2012.

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McGeer, Patrick L., Chikako Tanaka, and Yasuo Ihara. Neuroscientific Basis of Dementia. Birkhauser Verlag, 2012.

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(Editor), Chikako Tanaka, Patrick L. McGeer (Editor), and Yasuo Ihara (Editor), eds. Neuroscientific Basis of Dementia. Birkhauser, 2001.

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Book chapters on the topic "Beta barrel membrane proteins"

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Randall, Arlo, and Pierre Baldi. "Transmembrane beta-barrel protein structure prediction." In Structural Bioinformatics of Membrane Proteins, 83–102. Vienna: Springer Vienna, 2010. http://dx.doi.org/10.1007/978-3-7091-0045-5_5.

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Tsaousis, Georgios N., Stavros J. Hamodrakas, and Pantelis G. Bagos. "Predicting Beta Barrel Transmembrane Proteins Using HMMs." In Hidden Markov Models, 43–61. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6753-7_4.

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Van Du T. Tran, Philippe Chassignet, and Jean-Marc Steyaert. "Supersecondary Structure Prediction of Transmembrane Beta-Barrel Proteins." In Methods in Molecular Biology, 277–94. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-065-6_17.

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Kleinschmidt, Jörg H. "Folding and Stability of Monomeric β-Barrel Membrane Proteins." In Protein-Lipid Interactions, 27–56. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527606769.ch2.

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Leo, Jack C., Philipp Oberhettinger, and Dirk Linke. "Assessing the Outer Membrane Insertion and Folding of Multimeric Transmembrane β-Barrel Proteins." In Methods in Molecular Biology, 157–67. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2871-2_12.

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Gerlach, Lisa, Omkolsum Gholami, Nicole Schürmann, and Jörg H. Kleinschmidt. "Folding of β-Barrel Membrane Proteins into Lipid Membranes by Site-Directed Fluorescence Spectroscopy." In Methods in Molecular Biology, 465–92. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9512-7_20.

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Micsonai, András, Éva Bulyáki, and József Kardos. "BeStSel: From Secondary Structure Analysis to Protein Fold Prediction by Circular Dichroism Spectroscopy." In Methods in Molecular Biology, 175–89. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0892-0_11.

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Abstract Far-UV circular dichroism (CD) spectroscopy is a classical method for the study of the secondary structure of polypeptides in solution. It has been the general view that the α-helix content can be estimated accurately from the CD spectra. However, the technique was less reliable to estimate the β-sheet contents as a consequence of the structural variety of the β-sheets, which is reflected in a large spectral diversity of the CD spectra of proteins containing this secondary structure component. By taking into account the parallel or antiparallel orientation and the twist of the β-sheets, the Beta Structure Selection (BeStSel) method provides an improved β-structure determination and its performance is more accurate for any of the secondary structure types compared to previous CD spectrum analysis algorithms. Moreover, BeStSel provides extra information on the orientation and twist of the β-sheets which is sufficient for the prediction of the protein fold. The advantage of CD spectroscopy is that it is a fast and inexpensive technique with easy data processing which can be used in a wide protein concentration range and under various buffer conditions. It is especially useful when the atomic resolution structure is not available, such as the case of protein aggregates, membrane proteins or natively disordered chains, for studying conformational transitions, testing the effect of the environmental conditions on the protein structure, for verifying the correct fold of recombinant proteins in every scientific fields working on proteins from basic protein science to biotechnology and pharmaceutical industry. Here, we provide a brief step-by-step guide to record the CD spectra of proteins and their analysis with the BeStSel method.
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Schulz, Georg E. "Transmembrane β-barrel proteins." In Membrane Proteins, 47–70. Elsevier, 2003. http://dx.doi.org/10.1016/s0065-3233(03)63003-2.

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Hermansen, Simen, Dirk Linke, and Jack C. Leo. "Transmembrane β-barrel proteins of bacteria: From structure to function." In Membrane Proteins, 113–61. Elsevier, 2022. http://dx.doi.org/10.1016/bs.apcsb.2021.07.002.

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Stepanenko, Olesya V., Olga V. Stepanenko, Irina M. Kuznetsova, Vladislav V. Verkhusha, and Konstantin K. Turoverov. "Beta-Barrel Scaffold of Fluorescent Proteins." In International Review of Cell and Molecular Biology, 221–78. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-407699-0.00004-2.

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Conference papers on the topic "Beta barrel membrane proteins"

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Jimenez-Morales, David, Larisa Adamian, and Jie Liang. "Detecting remote homologues using scoring matrices calculated from the estimation of amino acid substitution rates of beta-barrel membrane proteins." In 2008 30th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2008. http://dx.doi.org/10.1109/iembs.2008.4649414.

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Tran, Van Du, Philippe Chassignet, Saad Sheikh, and Jean-Marc Steyaert. "Energy-based classification and structure prediction of transmembrane beta-barrel proteins." In 2011 IEEE 1st International Conference on Computational Advances in Bio and Medical Sciences (ICCABS). IEEE, 2011. http://dx.doi.org/10.1109/iccabs.2011.5729872.

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Zou, Lingyun, and Zhengzhi Wang. "Predicting Transmembrane Topology of β-barrel Membrane Proteins with A Hidden Markov Model." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.41.

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Jackups, Ronald, and Jie Liang. "Combinatorial model for sequence and spatial motif discovery in short sequence fragments: Examples from ß-barrel membrane proteins." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.259727.

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Jackups, Ronald, and Jie Liang. "Combinatorial model for sequence and spatial motif discovery in short sequence fragments: Examples from ß-barrel membrane proteins." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.4398193.

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Xian, Guangming, and Biqing-Zeng Xian. "A Novel Algorithm for Predicting '-barrel outer Membrane Proteins using ACO-based Hyper-parameter Selection for LS-SVMs." In 2012 National Conference on Information Technology and Computer Science. Paris, France: Atlantis Press, 2012. http://dx.doi.org/10.2991/citcs.2012.51.

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"Amyloidogenic properties of the beta-barrel proteins and their involvement in storage of nutrients in plant seeds and bacteria virulence." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-206.

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Piotrowicz, Randolph S., Kenneth M. Yamada, and Kunicki J. Kunicki. "HUMAN PLATELET GLYCOPROTEIN Ic-IIa IS AN ACTIVATION-INDEPENDENT FIBRONECTIN RECEPTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643911.

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Human platelets express the membrane glycoprotein (GP) heterodimer GPIIb-IIIa, which functions as an activation-dependent fibronectin (Fn) receptor. We have immunopurified the components of an activation-independent Fn receptor (FR) from human platelets employing a well-characterized rabbit polyclonal antibody raised against the beta chain of the chicken embryo fibroblast (CEF) FR (anti-band 3). This antibody crossreacts with antigen(s) expressed on both chicken thrombocytes and human platelets and inhibits the binding of both normal and thrombasthenic platelets (lacking GPIIb-IIIa) to Fn-coated surfaces in the absence of platelet activation.A monoclonal antibody directed against GPIIb-IIIa (AP2) partially inhibits the adhesion of normal platelets to Fn, but the combination of AP2 and anti-band 3 results in a level of inhibition greater than that obtained with either antibody alone. Thus, the presence of the FR alone is sufficient for the observed normal to enhanced binding of thrombasthenic platelets to Fn, whereas adhesion of normal platelets involves the synergistic action of the FR and GPIIb-IIIa. The adhesion of platelets to Fn mediated by the FR is inhibited by the tetrapeptide RGDS.Immunopurified FR appears to be a complex of two proteins: an alpha chain with an apparent molecular weight of 155/130 KD (nonreduced/reduced) and a beta chain with an apparent molecular weight of 125/147 KD. The alpha chain is composed of two subunits, dissociated by reduction, with electrophoretic mobilities identical to platelet glycoproteins previously designated lea and IcB. The beta chain comigrates with that platelet glycoprotein known as GPIIa. In an immunoblot assay, anti-band 3 binds to GPIIa but not to GPIc. The fact that anti-band 3 iramunoprecipitates both GP therefore suggests that they exist in a complex.Our findings establish GPIc-IIa as yet another platelet glycoprotein receptor complex and pave the way for future studies of the relative role of GPIIb-IIIa and GPIc-IIa in the adhesion of platelets to physiologic surfaces.
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